Structure of PDB 6z86 Chain O

Receptor sequence
>6z86O (length=191) Species: 9606 (Homo sapiens) [Search protein sequence]
SEEDNELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKGY
QETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLPN
KQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEAT
HMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS
3D structure
PDB6z86 A hybrid approach reveals the allosteric regulation of GTP cyclohydrolase I.
ChainO
Resolution2.206 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) C82 E83 H84 H85 Q123 H151 C153
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 O C141 H144 C212 C82 H85 C153
BS02 QBQ O N118 F122 G164 L165 S166 K167 R170 N59 F63 G105 L106 S107 K108 R111 MOAD: Kd=798uM
BS03 QBQ O C141 H143 H144 V181 Q182 E183 H210 R216 C82 H84 H85 V122 Q123 E124 H151 R157 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
PDBsum6z86
PubMed33229582
UniProtP30793|GCH1_HUMAN GTP cyclohydrolase 1 (Gene Name=GCH1)

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