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

7ZSR

purine nucleoside phosphorylase in complex with JS-379

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004731molecular_functionpurine-nucleoside phosphorylase activity
A0005737cellular_componentcytoplasm
A0006139biological_processnucleobase-containing compound metabolic process
A0006154biological_processadenosine catabolic process
A0006161biological_processdeoxyguanosine catabolic process
A0009116biological_processnucleoside metabolic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
B0003824molecular_functioncatalytic activity
B0004731molecular_functionpurine-nucleoside phosphorylase activity
B0005737cellular_componentcytoplasm
B0006139biological_processnucleobase-containing compound metabolic process
B0006154biological_processadenosine catabolic process
B0006161biological_processdeoxyguanosine catabolic process
B0009116biological_processnucleoside metabolic process
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
C0003824molecular_functioncatalytic activity
C0004731molecular_functionpurine-nucleoside phosphorylase activity
C0005737cellular_componentcytoplasm
C0006139biological_processnucleobase-containing compound metabolic process
C0006154biological_processadenosine catabolic process
C0006161biological_processdeoxyguanosine catabolic process
C0009116biological_processnucleoside metabolic process
C0016757molecular_functionglycosyltransferase activity
C0016763molecular_functionpentosyltransferase activity
Functional Information from PROSITE/UniProt
site_idPS01240
Number of Residues42
DetailsPNP_MTAP_2 Purine and other phosphorylases family 2 signature. LvlaGriHaYeghdLryvVhpVrAaraaGaqi.MVltNAaGGL
ChainResidueDetails
ALEU83-LEU124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:11444966, ECO:0007744|PDB:1G2O, ECO:0007744|PDB:1I80
ChainResidueDetails
ASER36
AARG88
ASER208
BSER36
BARG88
BSER208
CSER36
CARG88
CSER208

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P45563
ChainResidueDetails
AHIS68
AALA120
BHIS68
BALA120
CHIS68
CALA120

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:11444966
ChainResidueDetails
AGLU189
AASN231
BGLU189
BASN231
CGLU189
CASN231

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon