Structure of PDB 2a7r Chain B

Receptor sequence
>2a7rB (length=337) Species: 9606 (Homo sapiens) [Search protein sequence]
MPHIDNDVKLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPI
IAANMDTVGTFEMAKVLCKFSLFTAVHKHYSLVQWQEFAGQNPDCLEHLA
ASSGTGSSDFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRKRFP
QHTIMAGNVVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLS
AVMECADAAHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSE
SGGELIERDGKKYKLFYGMSSEMAMKKYAGGVAEYRSEGKTVEVPFKGDV
EHTIRDILGGIRSTCTYVGAAKLKELSRRTTFIRVTQ
3D structure
PDB2a7r Crystal Structure of Human Guanosine Monophosphate Reductase 2 (GMPR2) in Complex with GMP
ChainB
Resolution3.0 Å
3D
structure
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Enzymatic activity
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 B M55 G183 S184 C186 D219 G220 G242 G243 G268 S270 R286 S288 G290 M55 G183 S184 C186 D219 G220 G242 G243 G268 S270 R286 S287 G289
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:0046037 GMP metabolic process
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:2a7r, PDBe:2a7r, PDBj:2a7r
PDBsum2a7r
PubMed16359702
UniProtQ9P2T1|GMPR2_HUMAN GMP reductase 2 (Gene Name=GMPR2)

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