Structure of PDB 1fb1 Chain E

Receptor sequence
>1fb1E (length=196) Species: 9606 (Homo sapiens) [Search protein sequence]
GERPRSEEDNELNLPNLAAAYSSILSSLGENPQRQGLLKTPWRAASAMQF
FTKGYQETISDVLNDAIFDEDHDEMVIVKDIDMFSMCEHHLVPFVGKVHI
GYLPNKQVLGLSKLARIVEIYSRRLQVQERLTKQIAVAITEALRPAGVGV
VVEATHMCMVMRGVQKMNSKTVTSTMLGVFREDPKTREEFLTLIRS
3D structure
PDB1fb1 Zinc plays a key role in human and bacterial GTP cyclohydrolase I.
ChainE
Resolution3.1 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) C141 E142 H143 H144 Q182 H210 C212
Catalytic site (residue number reindexed from 1) C87 E88 H89 H90 Q128 H156 C158
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 E C141 H144 C212 C87 H90 C158
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:1fb1, PDBe:1fb1, PDBj:1fb1
PDBsum1fb1
PubMed11087827
UniProtP30793|GCH1_HUMAN GTP cyclohydrolase 1 (Gene Name=GCH1)

[Back to BioLiP]