Structure of PDB 2bzn Chain E

Receptor sequence
>2bznE (length=320) Species: 9606 (Homo sapiens) [Search protein sequence]
SLDFKDVLLRPKRSTLKSRSEVDLTRSFSFRNSKQTYSGVPIIAANMDTV
GTFEMAKVLCKFSLFTAVHKHYSLVQWQEFAGQNPDCLEHLAASSGTGSS
DFEQLEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGN
VVTGEMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADA
AHGLKGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIER
DGKKYKLFYGMSSEMAMKKYASEGKTVEVPFKGDVEHTIRDILGGIRSTC
TYVGAAKLKELSRRTTFIRV
3D structure
PDB2bzn Cofactor Mobility Determines Reaction Outcome in the Impdh and Gmpr (Beta-Alpha)(8) Barrel Enzymes.
ChainE
Resolution2.15 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 IMP E M55 G183 S184 C186 D219 G221 G242 G243 G268 M269 S270 E289 M47 G175 S176 C178 D211 G213 G234 G235 G260 M261 S262 E273
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:2bzn, PDBe:2bzn, PDBj:2bzn
PDBsum2bzn
PubMed22037469
UniProtQ9P2T1|GMPR2_HUMAN GMP reductase 2 (Gene Name=GMPR2)

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