3VM6
Crystal structure of ribose-1,5-bisphosphate isomerase from Thermococcus kodakarensis KOD1 in complex with alpha-D-ribose-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 SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 |
| Chain | Residue | Details |
| A | SER133 | |
| B | SER133 | |
| C | SER133 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 |
| Chain | Residue | Details |
| A | ASP202 | |
| B | ASP202 | |
| C | ASP202 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02230 |
| Chain | Residue | Details |
| A | ARG20 | |
| A | SER135 | |
| A | ASN212 | |
| B | ARG20 | |
| B | SER135 | |
| B | ASN212 | |
| C | ARG20 | |
| C | SER135 | |
| C | ASN212 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_02230, ECO:0000269|PubMed:22511789 |
| Chain | Residue | Details |
| A | ARG63 | |
| A | LYS238 | |
| B | ARG63 | |
| B | LYS238 | |
| C | ARG63 | |
| C | LYS238 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | SITE: Plays a key role in hexamerization |
| Chain | Residue | Details |
| A | ARG227 | |
| B | ARG227 | |
| C | ARG227 |
