1NUL
XPRTASE FROM E. COLI
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0000310 | molecular_function | xanthine phosphoribosyltransferase activity |
A | 0004422 | molecular_function | hypoxanthine phosphoribosyltransferase activity |
A | 0005829 | cellular_component | cytosol |
A | 0005886 | cellular_component | plasma membrane |
A | 0006166 | biological_process | purine ribonucleoside salvage |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0032263 | biological_process | GMP salvage |
A | 0032264 | biological_process | IMP salvage |
A | 0032265 | biological_process | XMP salvage |
A | 0032991 | cellular_component | protein-containing complex |
A | 0042802 | molecular_function | identical protein binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0051289 | biological_process | protein homotetramerization |
A | 0052657 | molecular_function | guanine phosphoribosyltransferase activity |
A | 0097216 | molecular_function | guanosine tetraphosphate binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0000310 | molecular_function | xanthine phosphoribosyltransferase activity |
B | 0004422 | molecular_function | hypoxanthine phosphoribosyltransferase activity |
B | 0005829 | cellular_component | cytosol |
B | 0005886 | cellular_component | plasma membrane |
B | 0006166 | biological_process | purine ribonucleoside salvage |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0032263 | biological_process | GMP salvage |
B | 0032264 | biological_process | IMP salvage |
B | 0032265 | biological_process | XMP salvage |
B | 0032991 | cellular_component | protein-containing complex |
B | 0042802 | molecular_function | identical protein binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0051289 | biological_process | protein homotetramerization |
B | 0052657 | molecular_function | guanine phosphoribosyltransferase activity |
B | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE SO4 B 301 |
Chain | Residue |
A | ARG53 |
B | SER36 |
B | ARG37 |
B | GLY38 |
B | LYS106 |
B | HOH762 |
B | HOH795 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 302 |
Chain | Residue |
A | HOH735 |
A | HOH777 |
A | HOH866 |
A | HOH960 |
A | ARG37 |
A | GLY38 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 501 |
Chain | Residue |
B | ASP89 |
B | HOH955 |
B | HOH956 |
B | HOH957 |
B | HOH958 |
B | HOH959 |
site_id | AC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG A 502 |
Chain | Residue |
A | ASP88 |
A | ASP89 |
A | HOH960 |
A | HOH961 |
A | HOH962 |
A | HOH963 |
A | HOH964 |
Functional Information from PROSITE/UniProt
site_id | PS00103 |
Number of Residues | 13 |
Details | PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. FIVIDDLVDTGgT |
Chain | Residue | Details |
A | PHE84-THR96 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000305|PubMed:9743633, ECO:0007744|PDB:1A95 |
Chain | Residue | Details |
A | ARG37 | |
A | ASP88 | |
B | ARG37 | |
B | ASP88 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A97 |
Chain | Residue | Details |
A | ARG69 | |
A | TRP134 | |
B | ARG69 | |
B | TRP134 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9100006 |
Chain | Residue | Details |
A | ASP89 | |
B | ASP89 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:9743633, ECO:0007744|PDB:1A96 |
Chain | Residue | Details |
A | ASP92 | |
A | ILE135 | |
B | ASP92 | |
B | ILE135 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
A | ASP92 | |
A | ASP88 | |
A | LYS115 | |
A | ASP89 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
B | ASP92 | |
B | ASP88 | |
B | LYS115 | |
B | ASP89 |
site_id | CSA3 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
A | ASP92 | |
A | ASP88 | |
A | ARG119 | |
A | LYS115 | |
A | ASP89 |
site_id | CSA4 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1a95 |
Chain | Residue | Details |
B | ASP92 | |
B | ASP88 | |
B | ARG119 | |
B | LYS115 | |
B | ASP89 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 391 |
Chain | Residue | Details |
A | ASP88 | electrostatic stabiliser |
A | ASP89 | electrostatic stabiliser |
A | ASP92 | proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 391 |
Chain | Residue | Details |
B | ASP88 | electrostatic stabiliser |
B | ASP89 | electrostatic stabiliser |
B | ASP92 | proton shuttle (general acid/base) |