3PNP
THE HIGH RESOLUTION CRYSTAL STRUCTURE OF BOVINE SPLEEN PURINE NUCLEOSIDE PHOSPHORYLASE IN COMPLEX FORMS WITH PHOSPHATE AND 9-DEAZAINOSINE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006139 | biological_process | nucleobase-containing compound metabolic process |
A | 0006166 | biological_process | purine ribonucleoside salvage |
A | 0009116 | biological_process | nucleoside metabolic process |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0016763 | molecular_function | pentosyltransferase activity |
A | 0047975 | molecular_function | guanosine phosphorylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 291 |
Chain | Residue |
A | HOH355 |
A | HOH360 |
A | HOH350 |
A | HOH351 |
A | HOH353 |
A | HOH354 |
site_id | AC2 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE PO4 A 290 |
Chain | Residue |
A | GLY32 |
A | SER33 |
A | HIS64 |
A | ARG84 |
A | HIS86 |
A | ASN115 |
A | ALA116 |
A | SER220 |
A | HOH301 |
A | HOH302 |
A | HOH303 |
A | HOH366 |
site_id | NUL |
Number of Residues | 5 |
Details | PHOSPHATE BINDING SITE. |
Chain | Residue |
A | HIS86 |
A | ARG84 |
A | SER33 |
A | SER220 |
A | ALA116 |
Functional Information from PROSITE/UniProt
site_id | PS01240 |
Number of Residues | 42 |
Details | PNP_MTAP_2 Purine and other phosphorylases family 2 signature. VmmqGrfHmYegypFwkvTfpVrVfrllGvet.LVvtNAaGGL |
Chain | Residue | Details |
A | VAL79-LEU120 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | SER33 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9585525, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9T, ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP |
Chain | Residue | Details |
A | HIS64 |
site_id | SWS_FT_FI3 |
Number of Residues | 3 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | ARG84 | |
A | ALA116 | |
A | SER220 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9585525, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T |
Chain | Residue | Details |
A | TYR88 | |
A | MET219 | |
A | HIS257 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: 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 |
Chain | Residue | Details |
A | GLU201 | |
A | ASN243 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Important for substrate specificity => ECO:0000250|UniProtKB:P00491 |
Chain | Residue | Details |
A | ASN243 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P00491 |
Chain | Residue | Details |
A | MET1 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00491 |
Chain | Residue | Details |
A | SER251 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1cg6 |
Chain | Residue | Details |
A | ASN243 | |
A | HIS86 | |
A | GLU89 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1cg6 |
Chain | Residue | Details |
A | ASN243 |