Structure of PDB 6z86 Chain N

Receptor sequence
>6z86N (length=193) Species: 9606 (Homo sapiens) [Search protein sequence]
PRSEEDNELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQFFTK
GYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHIGYL
PNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGVVVE
ATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS
3D structure
PDB6z86 A hybrid approach reveals the allosteric regulation of GTP cyclohydrolase I.
ChainN
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) C84 E85 H86 H87 Q125 H153 C155
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 N C141 H143 H144 V181 Q182 E183 H210 R216 C84 H86 H87 V124 Q125 E126 H153 R159 MOAD: Kd=798uM
BS02 ZN N C141 H144 C212 C84 H87 C155
BS03 QBQ N N118 F122 G164 L165 S166 K167 R170 N61 F65 G107 L108 S109 K110 R113 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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