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 | 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 | 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 | 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 | 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 | 10 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9743633","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1A95","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9100006","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9743633","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A97","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9743633","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1A96","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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) |
