5YFJ
Crystal structure of ribose-1,5-bisphosphate isomerase from Pyrococcus horikoshii OT3 in complex with ribulose-1,5-bisphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019323 | biological_process | pentose catabolic process |
| A | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| A | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
| A | 0046523 | molecular_function | S-methyl-5-thioribose-1-phosphate isomerase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0019323 | biological_process | pentose catabolic process |
| B | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| B | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
| B | 0046523 | molecular_function | S-methyl-5-thioribose-1-phosphate isomerase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0019323 | biological_process | pentose catabolic process |
| C | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| C | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
| C | 0046523 | molecular_function | S-methyl-5-thioribose-1-phosphate isomerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 22 |
| Details | binding site for residue RUB A 401 |
| Chain | Residue |
| A | MET19 |
| A | ALA139 |
| A | GLN166 |
| A | ALA203 |
| A | ASP204 |
| A | ASN214 |
| A | LYS215 |
| A | LYS240 |
| A | HOH542 |
| A | HOH546 |
| A | HOH552 |
| A | ARG22 |
| A | HOH555 |
| A | HOH559 |
| A | HOH583 |
| A | GLY23 |
| A | ALA24 |
| A | GLY25 |
| A | ARG65 |
| A | CYS135 |
| A | SER137 |
| A | LYS138 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue K A 402 |
| Chain | Residue |
| A | MET193 |
| A | LYS194 |
| A | THR196 |
| A | VAL230 |
| A | HOH591 |
| A | HOH646 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue CL A 403 |
| Chain | Residue |
| A | VAL251 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue PEG A 404 |
| Chain | Residue |
| A | PRO258 |
| A | LEU267 |
| A | LYS272 |
| A | GLU275 |
| A | VAL276 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue MPD A 405 |
| Chain | Residue |
| A | HOH505 |
| B | HOH664 |
| site_id | AC6 |
| Number of Residues | 22 |
| Details | binding site for residue RUB B 401 |
| Chain | Residue |
| B | MET19 |
| B | ARG22 |
| B | GLY23 |
| B | ALA24 |
| B | GLY25 |
| B | ARG65 |
| B | CYS135 |
| B | SER137 |
| B | LYS138 |
| B | ALA139 |
| B | GLN166 |
| B | ALA203 |
| B | ASP204 |
| B | ASN214 |
| B | LYS215 |
| B | LYS240 |
| B | HOH506 |
| B | HOH520 |
| B | HOH535 |
| B | HOH541 |
| B | HOH549 |
| B | HOH554 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue K B 402 |
| Chain | Residue |
| B | MET193 |
| B | LYS194 |
| B | THR196 |
| B | VAL230 |
| B | HOH631 |
| B | HOH636 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 403 |
| Chain | Residue |
| B | LEU250 |
| B | VAL251 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue PEG B 404 |
| Chain | Residue |
| B | TYR62 |
| B | PRO66 |
| B | GLU252 |
| B | HOH555 |
| site_id | AD1 |
| Number of Residues | 22 |
| Details | binding site for residue RUB C 401 |
| Chain | Residue |
| C | MET19 |
| C | ARG22 |
| C | GLY23 |
| C | ALA24 |
| C | GLY25 |
| C | ARG65 |
| C | CYS135 |
| C | SER137 |
| C | LYS138 |
| C | ALA139 |
| C | GLN166 |
| C | ALA203 |
| C | ASP204 |
| C | ASN214 |
| C | LYS215 |
| C | LYS240 |
| C | HOH511 |
| C | HOH515 |
| C | HOH517 |
| C | HOH523 |
| C | HOH542 |
| C | HOH563 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue K C 402 |
| Chain | Residue |
| C | MET193 |
| C | LYS194 |
| C | THR196 |
| C | VAL230 |
| C | HOH586 |
| C | HOH605 |
| site_id | AD3 |
| Number of Residues | 1 |
| Details | binding site for residue CL C 403 |
| Chain | Residue |
| C | VAL251 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_02230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_02230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
