Structure of PDB 2ble Chain A

Receptor sequence

>2bleA (length=337) Species: 9606 (Homo sapiens)

MPRIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPI
IVANMDTVGTFEMAAVMSQHSMFTAIHKHYSLDDWKLFATNHPECLQNVA
VSSGSGQNDLEKMTSILEAVPQVKFICLDVANGYSEHFVEFVKLVRAKFP
EHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLS
AVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTE
CAGEVIRKLKLFYGMSSDTAMNKHGVAEYRASEGKTVEVPYKGDVENTIL
DILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTV

3D structure

• PDB: 2ble Structure of Human Guanosine Monophosphate Reductase Gmpr1 in Complex with Gmp
• Chain: A
• Resolution: 1.9 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K13 I48 P49 C186 T188 E289
• Catalytic site (residue number reindexed from 1): K13 I48 P49 C186 T188 E283
• 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 G221 L241 G242 G243 G268 M269 S270 R286 S288 G290	M55 G183 S184 D219 G220 G221 L241 G242 G243 G264 M265 S266 R280 S282 G284

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

External links

• PDB: RCSB:2ble, PDBe:2ble, PDBj:2ble
• PDBsum: 2ble
• UniProt: P36959|GMPR1_HUMAN GMP reductase 1 (Gene Name=GMPR)