Structure of PDB 2qv6 Chain D

Receptor sequence
>2qv6D (length=253) Species: 2190 (Methanocaldococcus jannaschii) [Search protein sequence]
MIQITVIQIDNYGPWTVTPNPRRESDLQALQSRLYADLNLMFGAHKGLVF
YTRFDNLIAITNGIDLITHKRIQESIRNRYPFTVSMVIASAETPYEAQKL
ATETLQEYGSAQDENRKEVLDVANELVVDGYVQIAHIDINNITGTLTDIV
SAYDTYLNVNKVKLALMEELLKYNALLFFIGGDNFMAPSNGMSEEDFLDI
FNRINKKYKIELKAGIGIGRTAEDASNLADIGLEKIRGKLVDKNVCTLKQ
DDF
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
ChainD
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 K D R22 E24 R22 E24
BS02 GTP D Y12 T16 E24 L27 D55 Q112 Y12 T16 E24 L27 D55 Q112
BS03 K D H136 D230 H136 D230
BS04 CA D D138 I139 D183 D138 I139 D183
BS05 GTP D H136 D138 I139 N141 I142 T143 I180 D183 N184 K213 R237 H136 D138 I139 N141 I142 T143 I180 D183 N184 K213 R237
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

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Molecular Function
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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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