1PWY
CRYSTAL STRUCTURE OF HUMAN PNP COMPLEXED WITH ACYCLOVIR
Functional Information from GO Data
Chain | GOid | namespace | contents |
E | 0000255 | biological_process | allantoin metabolic process |
E | 0001882 | molecular_function | nucleoside binding |
E | 0002060 | molecular_function | purine nucleobase binding |
E | 0003824 | molecular_function | catalytic activity |
E | 0004731 | molecular_function | purine-nucleoside phosphorylase activity |
E | 0005515 | molecular_function | protein binding |
E | 0005576 | cellular_component | extracellular region |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0006139 | biological_process | nucleobase-containing compound metabolic process |
E | 0006148 | biological_process | inosine catabolic process |
E | 0006149 | biological_process | deoxyinosine catabolic process |
E | 0006157 | biological_process | deoxyadenosine catabolic process |
E | 0006166 | biological_process | purine ribonucleoside salvage |
E | 0006204 | biological_process | IMP catabolic process |
E | 0006738 | biological_process | nicotinamide riboside catabolic process |
E | 0006955 | biological_process | immune response |
E | 0009116 | biological_process | nucleoside metabolic process |
E | 0009165 | biological_process | nucleotide biosynthetic process |
E | 0009410 | biological_process | response to xenobiotic stimulus |
E | 0016757 | molecular_function | glycosyltransferase activity |
E | 0016763 | molecular_function | pentosyltransferase activity |
E | 0032743 | biological_process | positive regulation of interleukin-2 production |
E | 0034418 | biological_process | urate biosynthetic process |
E | 0034774 | cellular_component | secretory granule lumen |
E | 0042102 | biological_process | positive regulation of T cell proliferation |
E | 0042301 | molecular_function | phosphate ion binding |
E | 0042802 | molecular_function | identical protein binding |
E | 0043101 | biological_process | purine-containing compound salvage |
E | 0046059 | biological_process | dAMP catabolic process |
E | 0046638 | biological_process | positive regulation of alpha-beta T cell differentiation |
E | 0047975 | molecular_function | guanosine phosphorylase activity |
E | 0070062 | cellular_component | extracellular exosome |
E | 1904813 | cellular_component | ficolin-1-rich granule lumen |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 E 291 |
Chain | Residue |
E | GLY32 |
E | GLY34 |
E | LEU35 |
E | GLY36 |
E | GLN82 |
E | HOH295 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 E 292 |
Chain | Residue |
E | PRO92 |
E | GLN144 |
E | ARG148 |
site_id | AC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 E 293 |
Chain | Residue |
E | GLY32 |
E | SER33 |
E | ARG84 |
E | HIS86 |
E | ASN115 |
E | ALA116 |
E | SER220 |
E | HOH333 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE AC2 E 290 |
Chain | Residue |
E | ALA116 |
E | ALA117 |
E | GLY118 |
E | PHE200 |
E | GLU201 |
E | VAL217 |
E | MET219 |
E | THR242 |
E | ASN243 |
E | VAL245 |
E | HIS257 |
E | HOH300 |
Functional Information from PROSITE/UniProt
site_id | PS01240 |
Number of Residues | 42 |
Details | PNP_MTAP_2 Purine and other phosphorylases family 2 signature. VmmqGrfHmYegypLwkvTfpVrVfhllGvdt.LVvtNAaGGL |
Chain | Residue | Details |
E | VAL79-LEU120 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA |
Chain | Residue | Details |
E | SER33 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P55859 |
Chain | Residue | Details |
E | HIS64 |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:14706628, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULA, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:1V3Q, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA |
Chain | Residue | Details |
E | ARG84 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8 |
Chain | Residue | Details |
E | TYR88 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14706628, ECO:0000269|PubMed:23438750, ECO:0000305|PubMed:1763067, ECO:0007744|PDB:1RCT, ECO:0007744|PDB:1ULB, ECO:0007744|PDB:4EAR, ECO:0007744|PDB:4EB8, ECO:0007744|PDB:4GKA |
Chain | Residue | Details |
E | ALA116 | |
E | GLU201 | |
E | SER220 | |
E | ASN243 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:14706628, ECO:0007744|PDB:1RCT |
Chain | Residue | Details |
E | MET219 | |
E | HIS257 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | SITE: Important for substrate specificity => ECO:0000269|PubMed:9305964 |
Chain | Residue | Details |
E | ASN243 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
E | SER251 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ula |
Chain | Residue | Details |
E | ASN243 | |
E | HIS86 | |
E | GLU89 |
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 17 |
Chain | Residue | Details |
E | SER33 | hydrogen bond donor |
E | HIS257 | electrostatic stabiliser, hydrogen bond acceptor |
E | HIS64 | electrostatic stabiliser |
E | HIS86 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
E | TYR88 | electrostatic stabiliser, hydrogen bond donor |
E | GLU89 | activator, electrostatic stabiliser, hydrogen bond acceptor |
E | ALA116 | electrostatic stabiliser, hydrogen bond donor |
E | MET219 | electrostatic stabiliser, hydrogen bond donor |
E | SER220 | electrostatic stabiliser, hydrogen bond donor |
E | ASN243 | electrostatic stabiliser, hydrogen bond donor, polar interaction |