Structure of PDB 2qv6 Chain B

Receptor sequence
>2qv6B (length=250) Species: 2190 (Methanocaldococcus jannaschii) [Search protein sequence]
MIQITVIQIDNYGPWTVTPNPRRESDLQALQSRLYADLNLMFGAHKGLVF
YTRFDNLIAITNGIDLITHKRIQESIRNRYPFTVSMVIASAETPYEAQKL
ATETLQEYGSAQDENRKEVLDVANELVVDGYVQIAHIDINNITGTLTDIV
SAYDTYLNVNKVKLALMEELLKYNALLFFIGGDNFMAPSNGMSEEDFLDI
FNRINKKYKIELKAGIGIGRTAEDASNLADIGLEKIRGKLVDKNVCTLKQ
3D structure
PDB2qv6 A New Use for a Familiar Fold: The X-ray Crystal Structure of GTP-Bound GTP Cyclohydrolase III from Methanocaldococcus jannaschii Reveals a Two Metal Ion Catalytic Mechanism
ChainB
Resolution2.0 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.5.4.29: GTP cyclohydrolase IIa.
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 CA B D138 I139 D183 D138 I139 D183
BS02 GTP B H136 D138 N140 N141 I142 T143 I180 D183 N184 K213 R237 H136 D138 N140 N141 I142 T143 I180 D183 N184 K213 R237
BS03 K B R22 E24 R22 E24
BS04 GTP B Y12 T16 E24 L27 D55 Q112 Y12 T16 E24 L27 D55 Q112
Gene Ontology
Molecular Function
GO:0005525 GTP binding
GO:0016787 hydrolase activity
GO:0016814 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines
GO:0043740 GTP cyclohydrolase IIa activity
Biological Process
GO:0009058 biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:2qv6, PDBe:2qv6, PDBj:2qv6
PDBsum2qv6
PubMed18052207
UniProtQ57609|GCH3_METJA GTP cyclohydrolase III (Gene Name=gch3)

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