BioLiP

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

PDB

1a9c Atomic Structure of GTP Cyclohydrolase I

Chain

Resolution

2.9 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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Molecular Function

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Cellular Component

PDB	RCSB:1a9c, PDBe:1a9c, PDBj:1a9c
PDBsum	1a9c
PubMed
UniProt	P0A6T5\|GCH1_ECOLI GTP cyclohydrolase 1 (Gene Name=folE)