3A11
Crystal structure of ribose-1,5-bisphosphate isomerase from Thermococcus kodakaraensis KOD1
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 |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0019323 | biological_process | pentose catabolic process |
| D | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| D | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
| D | 0046523 | molecular_function | S-methyl-5-thioribose-1-phosphate isomerase activity |
| E | 0016853 | molecular_function | isomerase activity |
| E | 0019323 | biological_process | pentose catabolic process |
| E | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| E | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
| E | 0046523 | molecular_function | S-methyl-5-thioribose-1-phosphate isomerase activity |
| F | 0016853 | molecular_function | isomerase activity |
| F | 0019323 | biological_process | pentose catabolic process |
| F | 0019509 | biological_process | L-methionine salvage from methylthioadenosine |
| F | 0043917 | molecular_function | ribose 1,5-bisphosphate isomerase activity |
| F | 0046523 | molecular_function | S-methyl-5-thioribose-1-phosphate isomerase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG A 401 |
| Chain | Residue |
| A | LYS224 |
| A | ARG227 |
| A | VAL228 |
| A | TYR286 |
| A | ASP288 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG E 401 |
| Chain | Residue |
| A | GLU285 |
| A | TYR286 |
| E | LYS224 |
| E | ARG227 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG B 401 |
| Chain | Residue |
| B | LYS224 |
| B | VAL228 |
| B | THR230 |
| B | TYR286 |
| B | ASP288 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 411 |
| Chain | Residue |
| B | ASP304 |
| B | HOH678 |
| D | ASP304 |
| F | ASP304 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG C 401 |
| Chain | Residue |
| C | LYS224 |
| C | ARG227 |
| C | VAL228 |
| C | GLU285 |
| C | ASP288 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG D 401 |
| Chain | Residue |
| D | LYS224 |
| D | ARG227 |
| D | VAL228 |
| D | ASP288 |
| D | HOH619 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG E 411 |
| Chain | Residue |
| A | ASP304 |
| E | ASP304 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PEG F 401 |
| Chain | Residue |
| F | LYS224 |
| F | VAL228 |
| F | GLU285 |
| F | TYR286 |
| F | ASP288 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_02230","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22511789","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_02230","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22511789","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 36 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02230","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02230","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22511789","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Site: {"description":"Plays a key role in hexamerization"} |
| Chain | Residue | Details |
