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PDBsum entry 1a9c

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
1a9c
Jmol
Contents
Protein chains
(+ 9 more) 221 a.a. *
Ligands
GTP ×15
Waters ×630
* Residue conservation analysis
PDB id:
1a9c
Name: Hydrolase
Title: Gtp cyclohydrolase i (c110s mutant) in complex with gtp
Structure: Gtp cyclohydrolase i. Chain: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 562. Organ: brain. Expressed in: escherichia coli. Expression_system_taxid: 562. Other_details: homologous expression
Biol. unit: Homo-Decamer (from PDB file)
Resolution:
2.90Å     R-factor:   0.206     R-free:   0.288
Authors: G.Auerbach,H.Nar,A.Bracher,A.Bacher,R.Huber
Key ref: G.Auerbach et al. Gtp cyclohydrolase I in complex with gtp at 2.1 a resolution. To be published, .
Date:
04-Apr-98     Release date:   11-May-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P0A6T5  (GCH1_ECOLI) -  GTP cyclohydrolase 1
Seq:
Struc:
222 a.a.
221 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.3.5.4.16  - Gtp cyclohydrolase i.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Folate Biosynthesis (early stages)
      Reaction: GTP + H2O = formate + 2-amino-4-hydroxy-6-(erythro-1,2,3- trihydroxypropyl)-dihydropteridine triphosphate
GTP
Bound ligand (Het Group name = GTP)
corresponds exactly
+ 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
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     protein complex   2 terms 
  Biological process     metabolic process   5 terms 
  Biochemical function     catalytic activity     7 terms