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2AI2

Purine nucleoside phosphorylase from calf spleen

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004731molecular_functionpurine-nucleoside phosphorylase activity
A0005737cellular_componentcytoplasm
A0006139biological_processnucleobase-containing compound metabolic process
A0006166biological_processpurine ribonucleoside salvage
A0009116biological_processnucleoside metabolic process
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0047975molecular_functionguanosine phosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 290
ChainResidue
AHOH2000
AHOH2001
AHOH2002
AHOH2003
AHOH2007

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN A 291
ChainResidue
AHIS20
AHIS20
AHIS20

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 144 A 292
ChainResidue
AGLU52
AHOH2014
AHOH2040
AHOH2040
AHOH2101
AHOH2101
AHOH2152
AGLU52

site_idAC4
Number of Residues19
DetailsBINDING SITE FOR RESIDUE P1D A 293
ChainResidue
ASER33
AARG84
AHIS86
ATYR88
AASN115
AALA116
AGLY118
APHE200
AGLU201
AMET219
ASER220
ATHR242
AASN243
AHIS257
AVAL260
AHOH2004
AHOH2058
AHOH2080
AHOH2092

Functional Information from PROSITE/UniProt
site_idPS01240
Number of Residues42
DetailsPNP_MTAP_2 Purine and other phosphorylases family 2 signature. VmmqGrfHmYegypFwkvTfpVrVfrllGvet.LVvtNAaGGL
ChainResidueDetails
AVAL79-LEU120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:9585525, ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T, ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP
ChainResidueDetails
ASER33

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:9585525, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9T, ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP
ChainResidueDetails
AHIS64

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:9585525, ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R, ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T, ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP
ChainResidueDetails
AARG84
AALA116
ASER220

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:9585525, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T
ChainResidueDetails
ATYR88
AMET219
AHIS257

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:9585525, ECO:0000305|PubMed:9020983, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R, ECO:0007744|PDB:1VFN
ChainResidueDetails
AGLU201
AASN243

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Important for substrate specificity => ECO:0000250|UniProtKB:P00491
ChainResidueDetails
AASN243

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P00491
ChainResidueDetails
AMET1

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00491
ChainResidueDetails
ASER251

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
AASN243
AHIS86
AGLU89

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
AASN243
AASP248

222415

PDB entries from 2024-07-10

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