Structure of PDB 6z86 Chain Q

Receptor sequence
>6z86Q (length=190) Species: 9606 (Homo sapiens) [Search protein sequence]
RSEEDNELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTKG
YQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYLP
NKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVEA
THMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLI
3D structure
PDB6z86 A hybrid approach reveals the allosteric regulation of GTP cyclohydrolase I.
ChainQ
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) C83 E84 H85 H86 Q124 H152 C154
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 Q C141 H143 H144 V181 E183 R216 C83 H85 H86 V123 E125 R158 MOAD: Kd=798uM
BS02 ZN Q C141 H144 C212 C83 H86 C154
BS03 QBQ Q N118 F122 G164 L165 S166 K167 R170 N60 F64 G106 L107 S108 K109 R112 MOAD: Kd=798uM
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:6z86, PDBe:6z86, PDBj:6z86
PDBsum6z86
PubMed33229582
UniProtP30793|GCH1_HUMAN GTP cyclohydrolase 1 (Gene Name=GCH1)

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