_EC 3.5.4.16 Gtp cyclohydrolase i. 27 PDB entries  
EC 3.-.-.- Hydrolases. [21,057 PDB entries]
EC 3.5.-.- Acting on carbon-nitrogen bonds, other than peptide bonds. [1,666 PDB entries]
EC 3.5.4.- In cyclic amidines. [234 PDB entries]
EC 3.5.4.16 Gtp cyclohydrolase i. [27 PDB entries]    
1a8r

Pathway: Folate Biosynthesis (early stages)
Reaction: Gtp + H(2)O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3- trihydroxypropyl)-dihydropteridine triphosphate.
 


GTP
+ H(2)O
=
formate
+ 2-amino-4-hydroxy-6-(erythro-1,2,3- trihydroxypropyl)-dihydropteridine triphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site.

Comments: The reaction involves hydrolysis of two C-N bonds and isomerization of the pentose unit; the recyclization may be non-enzymic. Involved in the de novo synthesis of tetrahydrobiopterin from Gtp, with the other enzymes involved being Ec 1.1.1.153 and Ec 4.2.3.12.
Links:   [IntEnz]   [ExPASy]   [KEGG]  

There are 27 PDB entries in enzyme class E.C.3.5.4.16

  PDB code Protein
1a8r
Gtp cyclohydrolase i (h112s mutant) in complex with gtp
Source: Escherichia coli. Organism_taxid: 562. Organ: brain. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: homologous expression
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O (221 residues) CATH domains: 1.10.286.10 3.30.1130.10
Bound ligand:   Het Group GTP corresponds to enzyme reactant GTP
1a9c
Gtp cyclohydrolase i (c110s mutant) in complex with gtp
Source: Escherichia coli. Organism_taxid: 562. Organ: brain. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: homologous expression
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O (221 residues) CATH domains: 1.10.286.10 3.30.1130.10
Bound ligand:   Het Group GTP corresponds to enzyme reactant GTP
1fb1
Crystal structure of human gtp cyclohydrolase i
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: homo sapiens
Chains: A, B, C, D, E (196 residues) CATH domains: 1.10.286.10 3.30.1130.10
Bound ligand:   Het Group IPA is 40.00% similar to enzyme product Formate
1fbx
Crystal structure of zinc-containing e.Coli gtp cyclohydrolase i
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: escherichia coli
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O (221 residues) CATH domains: 1.10.286.10 3.30.1130.10
1gtp
Gtp cyclohydrolase i
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: homologous expression yes
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T (221 residues) CATH domains: 1.10.286.10 3.30.1130.10
1is7
Crystal structure of rat gtpchi/gfrp stimulatory complex
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H, I, J (194 residues) CATH domains: 1.10.286.10 3.30.1130.10
1is8
Crystal structure of rat gtpchi/gfrp stimulatory complex plus zn
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H, I, J (192 residues) CATH domains: 1.10.286.10 3.30.1130.10
1n3r
Biosynthesis of pteridins. Reaction mechanism of gtp cyclohydrolase i
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O (221 residues) CATH domains: 1.10.286.10 3.30.1130.10
Bound ligand:   Het Group GTP corresponds to enzyme reactant GTP
1n3s
Biosynthesis of pteridins. Reaction mechanism of gtp cyclohy
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H, I, J (221 residues) CATH domains: 1.10.286.10 3.30.1130.10
Bound ligand:   Het Group GTP corresponds to enzyme reactant GTP
1n3t
Biosynthesis of pteridins. Reaction mechanism of gtp cyclohydrolase i
Source: Escherichia coli. Organism_taxid: 562. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: F, G, H, I, J, K, L, M, N, O, A, B, C, D, E (221 residues) CATH domains: 1.10.286.10 3.30.1130.10
Bound ligand:   Het Group GTP corresponds to enzyme reactant GTP
1nmo
Structural genomics, protein ybgi, unknown function
Source: Escherichia coli, escherichia coli o15 ,. Organism_taxid: 562,83334. Strain: , o157:h7. Gene: ybgi or b0710 or z0861 or ecs0735. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (247 residues) CATH domains: 3.40.1390.30 3.40.1390.30
1nmp
Structural genomics, ybgi protein, unknown function
Source: Escherichia coli, escherichia coli o15 ,. Organism_taxid: 562,83334. Strain: , o157:h7. Gene: ybgi or b0710 or z0861 or ecs0735. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (247 residues) CATH domains: 3.40.1390.30 3.40.1390.30
1wm9
Structure of gtp cyclohydrolase i from thermus thermophilus
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E (185 residues) CATH domains: 1.10.286.10 3.30.1130.10
1wpl
Crystal structure of the inhibitory form of rat gtp cyclohydrolase i/gfrp complex
Source: Rattus norvegicus. Norway rat. Organism_taxid: 10116. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F, G, H, I, J (194 residues) CATH domains: 1.10.286.10 3.30.1130.10
Bound ligand:   Het Group HBI is 53.00% similar to enzyme reactant GTP
1wuq
Structure of gtp cyclohydrolase i complexed with 8-oxo-gtp
Source: Thermus thermophilus. Organism_taxid: 274. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D, E (184 residues) CATH domains: 1.10.286.10 3.30.1130.10
Bound ligand:   Het Group 8GT is 96.97% similar to enzyme reactant GTP
1wur
Structure of gtp cyclohydrolase i complexed with 8-oxo-dgtp
Source: Thermus thermophilus. Organism_taxid: 274. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C, D, E (185 residues) CATH domains: 1.10.286.10 3.30.1130.10
Bound ligand:   Het Group 8DG is 93.94% similar to enzyme reactant GTP
2fyw
Crystal structure of a conserved protein of unknown function streptococcus pneumoniae
Source: Streptococcus pneumoniae. Organism_taxid: 170187. Strain: tigr4. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C (267 residues) CATH domains: 3.40.1390.30 3.40.1390.30
2gx8
The crystal stucture of bacillus cereus protein related to n
Source: Bacillus cereus. Organism_taxid: 226900. Strain: atcc 14579. Gene: aap11199. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B, C (359 residues) CATH domains: Unassigned 3.30.70.830
2nyd
Crystal structure of staphylococcus aureus hypothetical prot
Source: Staphylococcus aureus subsp. Aureus. Organism_taxid: 158879. Strain: n315. Gene: sa1388. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (300 residues) CATH domains: Unassigned Unassigned
2r5r
The crystal structure of duf198 from nitrosomonas europaea atcc 19718
Source: Nitrosomonas europaea atcc 19718. Organism_taxid: 228410. Strain: ifo 14298. Gene: ne1163. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693.
Chain: A (246 residues) CATH domain: 3.10.270.10
2yyb
Crystal structure of ttha1606 from thermus thermophilus hb8
Source: Thermus thermophilus. Organism_taxid: 300852. Strain: hb8. Gene: ttha1606. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (242 residues) CATH domains: 3.40.1390.30 3.40.1390.30
3d1t
Crystal structure of gcyh-ib
Source: Neisseria gonorrhoeae. Organism_taxid: 485. Atcc: 700825. Gene: ngo0387. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (244 residues) CATH domain: 3.10.270.10
Bound ligand:   Het Group ACY is 75.00% similar to enzyme product Formate
3d2o
Crystal structure of manganese-metallated gtp cyclohydrolase type ib
Source: Neisseria gonorrhoeae. Organism_taxid: 485. Atcc: 700825. Gene: ngo0387. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B (244 residues) CATH domain: 3.10.270.10
3lnl
Crystal structure of staphylococcus aureus protein sa1388
Source: Staphylococcus aureus subsp. Aureus. Organism_taxid: 158879. Strain: n315. Gene: sa1388. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Chains: A, B (307 residues) CATH domains: Unassigned Unassigned
4du6
Crystal structure of gtp cyclohydrolase i from yersinia pest complexed with gtp
Source: Yersinia pseudotuberculosis. Organism_taxid: 214092. Strain: co92. Gene: fole, yptb1520. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Chains: A, B, C, D, E (219 residues) CATH domains: 1.10.286.10 3.30.1130.10
Bound ligand:   Het Group GTP corresponds to enzyme reactant GTP
4iwg
Crystal structure of the conserved hypothetical protein mj09 methanocaldococcus jannaschii (in c2221 form)
Source: Methanocaldococcus jannaschii. Organism_taxid: 243232. Strain: atcc 43067 / dsm 2661 / jal-1 / jcm 10045 / nbrc 10 gene: mj0927. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C (244 residues) CATH domains: Unassigned Unassigned
4iwm
Crystal structure of the conserved hypothetical protein mj09 methanocaldococcus jannaschii (in p21 form)
Source: Methanocaldococcus jannaschii. Organism_taxid: 243232. Strain: atcc 43067 / dsm 2661 / jal-1 / jcm 10045 / nbrc 10 gene: methanocaldococcus jannaschii, mj0927. Expressed in: escherichia coli. Expression_system_taxid: 562.
Chains: A, B, C, D, E, F (244 residues) CATH domains: Unassigned Unassigned