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PDBsum entry 6y9d

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protein ligands metals Protein-protein interface(s) links
Oxidoreductase PDB id
6y9d

 

 

 

 

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Contents
Protein chains
(+ 6 more) 352 a.a.
Ligands
FES ×12
152 ×12
SCN ×12
EPE ×12
Metals
_FE ×12
Waters ×1002
PDB id:
6y9d
Name: Oxidoreductase
Title: Crystal structure of the quaternary ammonium rieske monooxygenase cnta in complex with substrate l-carnitine
Structure: Carnitine monooxygenase oxygenase subunit. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Synonym: carnitine monooxygenase alpha subunit. Engineered: yes
Source: Acinetobacter baumannii. Organism_taxid: 470. Gene: anta_2, anta_1, anta_3, a7m79_02670, a7m90_13970, abuw_3074, b4r90_07590, b9x95_06095, bgc29_09330, c2u32_18540, c3415_14505, cbi29_00874, chq89_11265, cpi82_11190, csb70_0522, dli75_01970, dol94_04925, dva79_16365, e2533_13315, e2536_16135, e5294_15630, e5979_13670, ea685_07170, ea686_01565, ea706_03020, ea722_03860, ea746_003300, ewo92_12480, ewo96_16565, ewp49_15025, fd887_09300, fd913_14110, fju36_15000, fju42_16200, fju76_14830, fju79_08840,
Resolution:
1.97Å     R-factor:   0.212     R-free:   0.247
Authors: M.Quareshy,M.Shanmugam,T.D.Bugg,A.Cameron,Y.Chen
Key ref: M.Quareshy et al. Structural basis of carnitine monooxygenase cnta subs specificity, Inhibition and inter-Subunit electron tr. J biol chem, . PubMed id: 33158989
Date:
06-Mar-20     Release date:   18-Nov-20    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
A0A059ZPP5  (A0A059ZPP5_ACIBA) -  Carnitine monooxygenase oxygenase subunit from Acinetobacter baumannii
Seq:
Struc:
371 a.a.
352 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.1.14.13.239  - carnitine monooxygenase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: (R)-carnitine + NADH + O2 + H+ = (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
(R)-carnitine
+ NADH
+ O2
+ H(+)
= (3R)-3-hydroxy-4-oxobutanoate
+ trimethylamine
+ NAD(+)
+ H2O
Bound ligand (Het Group name = SCN)
matches with 40.00% similarity
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 

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