Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

8HUB

AMP deaminase 2 in complex with an inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0003876molecular_functionAMP deaminase activity
A0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
A0019239molecular_functiondeaminase activity
A0032264biological_processIMP salvage
B0003876molecular_functionAMP deaminase activity
B0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
B0019239molecular_functiondeaminase activity
B0032264biological_processIMP salvage
C0003876molecular_functionAMP deaminase activity
C0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
C0019239molecular_functiondeaminase activity
C0032264biological_processIMP salvage
D0003876molecular_functionAMP deaminase activity
D0009168biological_processpurine ribonucleoside monophosphate biosynthetic process
D0019239molecular_functiondeaminase activity
D0032264biological_processIMP salvage
Functional Information from PROSITE/UniProt
site_idPS00485
Number of Residues7
DetailsA_DEAMINASE Adenosine and AMP deaminase signature. SLSTDDP
ChainResidueDetails
ASER760-PRO766

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10104
ChainResidueDetails
APRO655
BPRO655
CPRO655
DPRO655

site_idSWS_FT_FI2
Number of Residues28
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AALA364
BLYS435
BPRO633
BHIS636
BGLY710
BLEU711
CALA364
CILE366
CLYS435
CPRO633
CHIS636
AILE366
CGLY710
CLEU711
DALA364
DILE366
DLYS435
DPRO633
DHIS636
DGLY710
DLEU711
ALYS435
APRO633
AHIS636
AGLY710
ALEU711
BALA364
BILE366

226262

PDB entries from 2024-10-16

PDB statisticsPDBj update infoContact PDBjnumon