Structure of PDB 1a9c Chain J

Receptor sequence
>1a9cJ (length=221) Species: 562 (Escherichia coli) [Search protein sequence]
PSLSKEAALVHEALVARGLETPLRPPVHEMDNETRKSLIAGHMTEIMQLL
NLDLADDSLMETPHRIAKMYVDEIFSGLDYANFPKITLIENKMKVDEMVT
VRDITLTSTSEHHFVTIDGKATVAYIPKDSVIGLSKINRIVQFFAQRPQV
QERLTQQILIALQTLLGTNNVAVSIDAVHYCVKARGIRDATSATTTTSLG
GLFKSSQNTRHEFLRAVRHHN
3D structure
PDB1a9c Atomic Structure of GTP Cyclohydrolase I
ChainJ
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S110 E111 H112 H113 Q151 H179 C181
Catalytic site (residue number reindexed from 1) S110 E111 H112 H113 Q151 H179 C181
Enzyme Commision number 3.5.4.16: GTP cyclohydrolase I.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GTP J T87 G133 L134 S135 K136 R139 T87 G133 L134 S135 K136 R139
BS02 GTP J H112 H113 V150 E152 R185 H112 H113 V150 E152 R185
Gene Ontology
Molecular Function
GO:0003934 GTP cyclohydrolase I activity
GO:0005525 GTP binding
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0042802 identical protein binding
GO:0046872 metal ion binding
Biological Process
GO:0006729 tetrahydrobiopterin biosynthetic process
GO:0006730 one-carbon metabolic process
GO:0008616 queuosine biosynthetic process
GO:0046654 tetrahydrofolate biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Cellular Component
External links
PDB RCSB:1a9c, PDBe:1a9c, PDBj:1a9c
PDBsum1a9c
PubMed
UniProtP0A6T5|GCH1_ECOLI GTP cyclohydrolase 1 (Gene Name=folE)

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