6MC0
Crystal Structure of Ribose-5-phosphate Isomerase from Legionella pneumophila with Bound Substrate Ribose-5-Phosphate and Product Ribulose-5-Phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004751 | molecular_function | ribose-5-phosphate isomerase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006014 | biological_process | D-ribose metabolic process |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0044281 | biological_process | small molecule metabolic process |
| B | 0004751 | molecular_function | ribose-5-phosphate isomerase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006014 | biological_process | D-ribose metabolic process |
| B | 0006098 | biological_process | pentose-phosphate shunt |
| B | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0044281 | biological_process | small molecule metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue R5P A 301 |
| Chain | Residue |
| A | THR26 |
| A | GLY95 |
| A | GLY96 |
| A | ALA97 |
| A | GLU101 |
| A | LYS119 |
| A | HOH427 |
| A | HOH483 |
| A | HOH510 |
| A | HOH526 |
| A | HOH529 |
| A | SER28 |
| A | THR29 |
| A | ASP79 |
| A | GLY80 |
| A | ALA81 |
| A | ASP82 |
| A | LYS92 |
| A | GLY93 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 302 |
| Chain | Residue |
| A | ASN185 |
| A | ILE187 |
| A | VAL190 |
| B | VAL191 |
| B | HOH442 |
| B | HOH474 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | binding site for residue 5RP B 301 |
| Chain | Residue |
| B | THR26 |
| B | SER28 |
| B | THR29 |
| B | ASP79 |
| B | GLY80 |
| B | ALA81 |
| B | ASP82 |
| B | LYS92 |
| B | GLY93 |
| B | GLY94 |
| B | GLY95 |
| B | GLY96 |
| B | ALA97 |
| B | LEU98 |
| B | GLU101 |
| B | LYS119 |
| B | HOH414 |
| B | HOH466 |
| B | HOH471 |
| B | HOH482 |
| B | HOH504 |
| B | HOH521 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 302 |
| Chain | Residue |
| A | VAL191 |
| A | HOH442 |
| A | HOH451 |
| B | ASN185 |
| B | ILE187 |
| B | VAL190 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00170 |
| Chain | Residue | Details |
| A | GLU101 | |
| B | GLU101 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00170 |
| Chain | Residue | Details |
| A | THR26 | |
| A | ASP79 | |
| A | LYS92 | |
| A | LYS119 | |
| B | THR26 | |
| B | ASP79 | |
| B | LYS92 | |
| B | LYS119 |
