Structure of PDB 2bzn Chain H

Receptor sequence
>2bznH (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.
ChainH
Resolution2.15 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 H M55 G183 S184 C186 D219 G220 G221 G242 G243 G268 M269 S270 E289 M47 G175 S176 C178 D211 G212 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2bzn, PDBe:2bzn, PDBj:2bzn
PDBsum2bzn
PubMed22037469
UniProtQ9P2T1|GMPR2_HUMAN GMP reductase 2 (Gene Name=GMPR2)

[Back to BioLiP]