Structure of PDB 2bzn Chain B

Receptor sequence
>2bznB (length=317) Species: 9606 (Homo sapiens) [Search protein sequence]
SLDFKDVLLRPKRSTLEVDLTRSFSFRNSKQTYSGVPIIAANMDTVGTFE
MAKVLCKFSLFTAVHKHYSLVQWQEFAGQNPDCLEHLAASSGTGSSDFEQ
LEQILEAIPQVKYICLDVANGYSEHFVEFVKDVRKRFPQHTIMAGNVVTG
EMVEELILSGADIIKVGIGPGSVCTTRKKTGVGYPQLSAVMECADAAHGL
KGHIISDGGCSCPGDVAKAFGAGADFVMLGGMLAGHSESGGELIERDGKK
YKLFYGMSSEMAMKKYASEGKTVEVPFKGDVEHTIRDILGGIRSTCTYVG
AAKLKELSRRTTFIRVT
3D structure
PDB2bzn Cofactor Mobility Determines Reaction Outcome in the Impdh and Gmpr (Beta-Alpha)(8) Barrel Enzymes.
ChainB
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 B M55 G183 S184 C186 D219 G220 G221 G242 G243 G268 M269 S270 E289 M43 G171 S172 C174 D207 G208 G209 G230 G231 G256 M257 S258 E269
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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