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

1A9P

BOVINE PURINE NUCLEOSIDE PHOSPHORYLASE COMPLEXED WITH 9-DEAZAINOSINE AND PHOSPHATE

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
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0047975molecular_functionguanosine phosphorylase activity
Functional Information from PDB Data
site_id9NE
Number of Residues6
Details
ChainResidue
ATYR88
AGLU201
AMET219
AASN243
AHIS257
AGLU259

site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE PO4 A 291
ChainResidue
AGLY32
ASER33
AHIS64
AARG84
AHIS86
AASN115
AALA116
ASER220
A9DI290
AHOH311

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE 9DI A 290
ChainResidue
AHIS86
ATYR88
AALA116
AGLY118
APHE200
AGLU201
AMET219
ATHR242
AASN243
AHIS257
AGLU259
APO4291

site_idPNG
Number of Residues6
Details
ChainResidue
AHIS86
AALA116
ASER220
ASER33
AHIS64
AARG84

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
AMET219
AHIS257
ATYR88

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

218500

PDB entries from 2024-04-17

PDB statisticsPDBj update infoContact PDBjnumon