Structure of PDB 6z85 Chain G

Receptor sequence
>6z85G (length=155) Species: 9606 (Homo sapiens) [Search protein sequence]
NLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGYDEMVIVK
DIDMFSMCEHHLVPFVGKVHIGYLPNKQVLGLSKLARIVEIYSRRLQVQE
RLTKQIAVAITEALRPAGVGVVVEATHMCKTVTSTMLGVFREDPKTREEF
LTLIR
3D structure
PDB6z85 A hybrid approach reveals the allosteric regulation of GTP cyclohydrolase I.
ChainG
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) C141 E142 H143 H144 Q182 H210 C212
Catalytic site (residue number reindexed from 1) C58 E59 H60 H61 Q99 H127 C129
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 ZN G C141 H144 C212 C58 H61 C129
BS02 HBI G D127 L157 T240 E243 D44 L74 T146 E149
BS03 HBI G R235 R241 R141 R147
Gene Ontology
Molecular Function
GO:0003934 GTP cyclohydrolase I activity
Biological Process
GO:0046654 tetrahydrofolate biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:6z85, PDBe:6z85, PDBj:6z85
PDBsum6z85
PubMed33229582
UniProtP30793|GCH1_HUMAN GTP cyclohydrolase 1 (Gene Name=GCH1)

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