Structure of PDB 2bwg Chain A

Receptor sequence
>2bwgA (length=335) Species: 9606 (Homo sapiens) [Search protein sequence]
PRIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPII
VANMDTVGTFEMAAVMSQHSMFTAIHKHYSLDDWKLFATNHPECLQNVAV
SSGSGQNDLEKMTSILEAVPQVKFICLDVANGYSEHFVEFVKLVRAKFPE
HTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSA
VIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTEC
AGEVIERNGRKLKLFYGMSSDTAMNKHGVAEYRASEGKTVEVPYKGDVEN
TILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQ
3D structure
PDB2bwg Structure of Human Guanosine Monophosphate Reductase Gmpr1 in Complex with Gmp
ChainA
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K13 I48 P49
Catalytic site (residue number reindexed from 1) K12 I47 P48
Enzyme Commision number 1.7.1.7: GMP reductase.
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 5GP A M55 G183 S184 D219 G220 G242 G243 G268 M269 S270 R286 S288 G290 M54 G182 S183 D218 G219 G241 G242 G267 M268 S269 R283 S285 G287
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0003920 GMP reductase activity
GO:0005515 protein binding
GO:0016491 oxidoreductase activity
GO:0046872 metal ion binding
Biological Process
GO:0006144 purine nucleobase metabolic process
GO:0006163 purine nucleotide metabolic process
GO:0009117 nucleotide metabolic process
GO:0009409 response to cold
Cellular Component
GO:0005829 cytosol
GO:1902560 GMP reductase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2bwg, PDBe:2bwg, PDBj:2bwg
PDBsum2bwg
PubMed
UniProtP36959|GMPR1_HUMAN GMP reductase 1 (Gene Name=GMPR)

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