Structure of PDB 6z86 Chain T

Receptor sequence

>6z86T (length=186) Species: 9606 (Homo sapiens) [Search protein sequence]

NELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYQETI
SDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPNKQVL
GLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEATHMCM
VMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIR

3D structure

PDB

6z86 A hybrid approach reveals the allosteric regulation of GTP cyclohydrolase I.

Chain

Resolution

2.206 Å

3D
structure

Catalytic site residues are labeled in the structure
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Enzymatic activity

Catalytic site (original residue number in PDB)	C141 E142 H143 H144 Q182 H210 C212
Catalytic site (residue number reindexed from 1)	C78 E79 H80 H81 Q119 H147 C149
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	QBQ	T	C141 H143 H144 V181 Q182 E183 H210 R216	C78 H80 H81 V118 Q119 E120 H147 R153	MOAD: Kd=798uM
BS02	ZN	T	C141 H144 C212	C78 H81 C149
BS03	QBQ	T	N118 F122 G164 L165 S166 K167 R170	N55 F59 G101 L102 S103 K104 R107	MOAD: Kd=798uM

Gene Ontology

	Molecular Function
GO:0003934	GTP cyclohydrolase I activity

	Biological Process
GO:0046654	tetrahydrofolate biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process

External links

PDB	RCSB:6z86, PDBe:6z86, PDBj:6z86
PDBsum	6z86
PubMed	33229582
UniProt	P30793\|GCH1_HUMAN GTP cyclohydrolase 1 (Gene Name=GCH1)

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