_EC 1.14.99.3 Heme oxygenase (biliverdin-producing). 67 PDB entries  
EC 1.-.-.- Oxidoreductases. [8,596 PDB entries]
EC 1.14.-.- Acting on paired donors, with incorporation or reduction of molecu [1,404 PDB entries]
EC 1.14.99.- Miscellaneous (requires further characterization). [149 PDB entries]
EC 1.14.99.3 Heme oxygenase (biliverdin-producing). [67 PDB entries]    
1dve

Reaction: Protoheme + 3 AH(2) + 3 O(2) = biliverdin + Fe(2+) + Co + 3 a + 3 H(2)O.
 


Protoheme
+ 3 × AH(2)
+
3 × O(2)
=
biliverdin
+ Fe(2+)
+
CO
+ 3 × A
+ 3 × H(2)O
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Other name(s): Heme oxidase. Heme oxygenase. Heme oxygenase (decyclizing).
Comments: Requires NAD(P)H and Ec 1.6.2.4. The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and b of biliverdin are derived from two separate oxygen molecules. The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to Co. The central iron is kept in the reduced state by NAD(P)H.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 67 PDB entries in enzyme class E.C.1.14.99.3

  PDB code Protein
1dve
Crystal structure of rat heme oxygenase-1 in complex with heme
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: expressed as residues 1-267
Chain: A (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1dvg
Crystal structure of rat heme oxygenase-1 in complex with heme; seleleno-methionine derivative, mutated at m51t,m93l, m155l,m191l.
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: expressed as residues 1-267
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1irm
Crystal structure of apo heme oxygenase-1
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: C, A, B (196 residues) CATH domain: 1.20.910.10
1ivj
Crystal structure of rat hemeoxygenase-1 in complex with hem azide.
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (212 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1iw0
Crystal structure of a heme oxygenase (hmuo) from corynebacterium diphtheriae complexed with heme in the ferric state
Source: Corynebacterium diphtheriae. Organism_taxid: 1717. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C (207 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1iw1
Crystal structure of a heme oxygenase (hmuo) from corynebacterium diphtheriae complexed with heme in the ferrous state
Source: Corynebacterium diphtheriae. Organism_taxid: 1717. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C (212 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1ix3
Crystal structure of rat heme oxygenase-1 in complex with heme bound to cyanide
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (222 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1ix4
Crystal structure of rat heme oxygenase-1 in complex with heme bound to carbon monoxide
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (212 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
  Het Group CMO corresponds to enzyme product CO
1j02
Crystal structure of rat heme oxygenase-1-heme bound to no
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (212 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1j2c
Crystal structure of rat heme oxygenase-1 in complex with biliverdin ixalpha-iron cluster
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (216 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group BLA is 86.00% similar to enzyme product biliverdin
1n3u
Crystal structure of human heme oxygenase 1 (ho-1) in complex with its substrate heme, crystal form b
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1n45
X-ray crystal structure of human heme oxygenase-1 (ho-1) in complex with its substrate heme
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1ni6
Comparisions of the heme-free and-bound crystal structures of human heme oxygenase-1
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, C, D (215 residues) CATH domain: 1.20.910.10
1oyk
Crystal structures of the ferric, ferrous, and ferrous-no forms of the asp140ala mutant of human heme oxygenase-1: catalytic implications
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1oyl
Crystal structures of the ferric, ferrous, and ferrous-no forms of the asp140ala mutant of human heme oxygenase-1: catalytic implications
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: B ( residues)
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1oze
Crystal structures of the ferric, ferrous, and ferrous-no forms of the asp140ala mutant of human heme oxygenase- 1:catalytic implications
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1ozl
Crystal structures of the ferric, ferrous, and ferrous-no forms of the asp140ala mutant of human heme oxygenase-1: catalytic implications
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1ozr
Crystal structures of the ferric, ferrous and ferrous-no forms of the asp140ala mutant of human heme oxygenase-1: catalytic implications
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1ozw
Crystal structures of the ferric, ferrous and ferrous-no forms of the asp140ala mutant of human heme oxygenase-1: catalytic implications
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1qq8
X-ray crystal structure of human heme oxygenase-1 (ho-1) in complex with its substrate heme
Source: Homo sapiens. Human. Expressed in: e.Coli
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Heme
1s13
Human heme oxygenase oxidatition of alpha- and gamma-meso- phenylhemes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1 or ho1 or ho. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: B ( residues)
Bound ligand:   Het Group 2FH is 68.00% similar to enzyme reactant Protoheme IX
1s8c
Crystal structure of human heme oxygenase in a complex with biliverdine
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho1, ho. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, D (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group BLA corresponds to enzyme product biliverdin
1t5p
Human heme oxygenase oxidation of alpha- and gamma-meso- phenylhemes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho1, ho. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (203 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group 1FH is 84.00% similar to enzyme reactant Protoheme IX
1twn
Crystal structures of ferrous and ferrous-no forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho1, ho. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group VER is 81.00% similar to enzyme product biliverdin
1twr
Crystal structures of ferrous and ferrous-no forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho1, ho. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group VER is 84.00% similar to enzyme product biliverdin
1ubb
Crystal structure of rat ho-1 in complex with ferrous heme
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (212 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1ulx
Partially photolyzed structure of co-bound heme-heme oxygenase complex
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (212 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
  Het Group CMO corresponds to enzyme product CO
1v8x
Crystal structure of the dioxygen-bound heme oxygenase from corynebacterium diphtheriae
Source: Corynebacterium diphtheriae. Organism_taxid: 1717. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (210 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
  Het Group OXY corresponds to enzyme reactant O(2)
1vgi
Crystal structure of xenon bound rat heme-heme oxygenase-1 complex
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (212 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
  Het Group FMT is 66.00% similar to enzyme product CO
1we1
Crystal structure of heme oxygenase-1 from cyanobacterium synechocystis sp. Pcc6803 in complex with heme
Source: Synechocystis sp.. Organism_taxid: 1148. Strain: pcc 6803. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D (222 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
  Het Group IPA is 50.00% similar to enzyme product CO
1wnv
D136a mutant of heme oxygenase from corynebacterium diphtheriae (hmuo)
Source: Corynebacterium diphtheriae. Organism_taxid: 1717. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C (207 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1wnw
D136n mutant of heme oxygenase from corynebacterium diphtheriae (hmuo)
Source: Corynebacterium diphtheriae. Organism_taxid: 1717. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: B, C ( residues)
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1wnx
D136e mutant of heme oxygenase from corynebacterium diphtheriae (hmuo)
Source: Corynebacterium diphtheriae. Organism_taxid: 1717. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: B ( residues)
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1wov
Crystal strucure of heme oxygenase-2 from synechocystis sp. Pcc 6803 in complex with heme
Source: Synechocystis sp. Pcc 6803. Organism_taxid: 1148. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (244 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1wow
Crystal structure of heme oxygenase-2 from synechocystis sp. Complexed with heme in ferrous form
Source: Synechocystis sp.. Organism_taxid: 1148. Strain: pcc 6803. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (245 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
1wox
Crystal structure of heme oxygenase-2 from synechocystis sp. In complex with heme and no
Source: Synechocystis sp.. Organism_taxid: 1148. Strain: pcc 6803. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (244 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
1wzf
Crystal structure of an artificial metalloprotein: fe(10-coo salophen)/wild type heme oxygenase
Source: Corynebacterium diphtheriae. Organism_taxid: 1717. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (209 residues) CATH domain: 1.20.910.10
1wzg
Crystal structure of an artificial metalloprotein: fe(saloph type heme oxygenase
Source: Corynebacterium diphtheriae. Organism_taxid: 1717. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chain: A (209 residues) CATH domain: 1.20.910.10
1xjz
Crystal structures of the g139a, g139a-no and g143h mutants of human heme oxygenase-1
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho1, ho. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1xk0
Crystal structures of the g139a, g139a-no and g143h mutants of human heme oxygenase-1
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho1, ho. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1xk1
Crystal structures of the g139a, g139a-no and g143h mutants of human heme oxygenase-1
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho1, ho. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1xk2
NADPH- and ascorbate-supported heme oxygenase reactions are distinct. Regiospecificity of heme cleavage by the r183e mutant
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho1, ho. Expressed in: escherichia coli. Expression_system_taxid: 562
Chain: A (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
1xk3
NADPH- and ascorbate-supported heme oxygenase reactions are distinct. Regiospecificity of heme cleavage by the r183e mutant
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho1, ho. Expressed in: escherichia coli. Expression_system_taxid: 562
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
2dy5
Crystal structure of rat heme oxygenase-1 in complex with heme and 2-[2-(4-chlorophenyl)ethyl]-2-[(1h-imidazol-1-yl) methyl]-1,3-dioxolane
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
2e7e
Bent-binding of cyanide to the heme iron in rat heme oxygenase-1
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (212 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
2q32
Crystal structure of human heme oxygenase-2 c127a (ho-2)
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hs.284279, hmox2, ho2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (213 residues) CATH domain: 1.20.910.10
2qpp
Crystal structure of human heme oxygenase-2 c127a (ho-2) wit heme
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox2, ho2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
2rgz
Ensemble refinement of the protein crystal structure of huma oxygenase-2 c127a (ho-2) with bound heme
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox2, ho2. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chain: A (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
2zvu
Crystal structure of rat heme oxygenase-1 in complex with ferrous verdoheme
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (212 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group VEA is 95.00% similar to enzyme product biliverdin
  Het Group FMT is 66.00% similar to enzyme product CO
3czy
Crystal structure of human heme oxygenase-1 in complex with 1-(adamantan-1-yl)-2-(1h-imidazol-1-yl)ethanone
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho, ho1. Expressed in: escherichia coli.
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
3hok
X-ray crystal structure of human heme oxygenase-1 with (2r, 4s)-2-[2-(4-chlorophenyl)ethyl]-2-[(1h-imidazol-1-yl) methyl]-4[((5-trifluoromethylpyridin-2-yl)thio)methyl]-1,3- dioxolane: a novel, inducible binding mode
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho, ho1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
3hx9
Structure of heme-degrader, mhud (rv3592), from mycobacterium tuberculosis with two hemes bound in its active site
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Strain: h37rv. Gene: mt3698, rv3592, tb11.2. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (101 residues) CATH domain: 3.30.70.900
3i9t
Crystal structure of the rat heme oxygenase (ho-1) in comple heme binding dithiothreitol (dtt)
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (212 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
3i9u
Crystal structure of the rat heme oxygenase (ho-1) in comple heme binding dithioerythritol (dte)
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (212 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
3k4f
X-ray crystal structure of human heme oxygenase-1 in complex with 4-phenyl-1-(1h-1,2,4-triazol-1-yl)-2-butanone
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho, ho1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (214 residues) CATH domain: 1.20.910.10
Bound ligand:   Het Group HEM is 95.00% similar to enzyme reactant Protoheme IX
3tgm
X-ray crystal structure of human heme oxygenase-1 in complex (1h-imidazol-1-yl)-4,4-diphenyl-2 butanone
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hmox1, ho, ho1. Expressed in: escherichia coli. Expression_system_taxid: 668369.
Chain: B ( residues)
Bound ligand:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
3wkt
Complex structure of an open form of NADPH-cytochrome p450 r and heme oxygenase-1
Source: Rattus norvegicus. Brown rat,rat,rats. Organism_taxid: 10116. Gene: por. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: hmox1.
Chains: C, D (214 residues)
Bound ligand:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
4g7l
Crystal structure of rat heme oxygenase-1 in complex with he
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (213 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
  Het Group OXY corresponds to enzyme reactant O(2)
  Het Group FMT is 66.67% similar to enzyme product CO
4g7p
Rat heme oxygenase-1 in complex with heme and co with 1 hr illumination at 100 k: laser off
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (213 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
  Het Group CMO corresponds to enzyme product CO
4g7t
Rat heme oxygenase-1 in complex with heme and co with 1 hr illumination: laser on
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (212 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
  Het Group FMT is 66.67% similar to enzyme product CO
4g7u
Rat heme oxygenase-1 in complex with heme and co with 16 hr illumination: laser off
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (213 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
  Het Group CMO corresponds to enzyme product CO
4g8p
Rat heme oxygenase-1 in complex with heme and co with 16 hr illumination: laser on
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (213 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
  Het Group FMT is 66.67% similar to enzyme product CO
4g8u
Rat heme oxygenase-1 in complex with heme and o2 with 13 hr illumination: laser off
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (213 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
  Het Group OXY corresponds to enzyme reactant O(2)
  Het Group FMT is 66.67% similar to enzyme product CO
4g8w
Rat heme oxygenase-1 in complex with heme and o2 with 13 hr illumination: laser on
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (213 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
  Het Group OXY corresponds to enzyme reactant O(2)
  Het Group FMT is 66.67% similar to enzyme product CO
4g98
Rat heme oxygenase-1 in complex with heme and co at 100k
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (212 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
  Het Group CMO corresponds to enzyme product CO
4g99
Rat heme oxygenase-1 in complex with heme and co at 100 k af warming to 160 k
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: hmox1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chain: A (212 residues) CATH domain: 1.20.910.10
Bound ligands:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
  Het Group CMO corresponds to enzyme product CO
4nl5
Mycobacterium tuberculosis heme-degrading protein mhud in co heme and cyanide
Source: Mycobacterium tuberculosis. Organism_taxid: 1773. Strain: h37rv. Gene: mhud, mt3698, rv3592. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Chains: A, B (101 residues)
Bound ligands:   Het Group HEM is 95.45% similar to enzyme reactant Protoheme
  Het Group ACT is 50.00% similar to enzyme product CO