4X84
Crystal structure of Ribose-5-phosphate isomerase A from Pseudomonas aeruginosa
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 |
| C | 0004751 | molecular_function | ribose-5-phosphate isomerase activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006014 | biological_process | D-ribose metabolic process |
| C | 0006098 | biological_process | pentose-phosphate shunt |
| C | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0044281 | biological_process | small molecule metabolic process |
| D | 0004751 | molecular_function | ribose-5-phosphate isomerase activity |
| D | 0005829 | cellular_component | cytosol |
| D | 0006014 | biological_process | D-ribose metabolic process |
| D | 0006098 | biological_process | pentose-phosphate shunt |
| D | 0009052 | biological_process | pentose-phosphate shunt, non-oxidative branch |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0044281 | biological_process | small molecule metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | binding site for residue FLC A 300 |
| Chain | Residue |
| A | THR32 |
| A | LYS125 |
| A | HOH502 |
| A | HOH507 |
| A | HOH514 |
| A | HOH521 |
| A | HOH579 |
| A | HOH585 |
| A | HOH705 |
| A | SER34 |
| A | THR35 |
| A | ALA87 |
| A | ASP88 |
| A | LYS98 |
| A | GLY99 |
| A | GLY100 |
| A | GLY101 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue FLC B 300 |
| Chain | Residue |
| B | THR32 |
| B | SER34 |
| B | THR35 |
| B | ALA87 |
| B | ASP88 |
| B | LYS98 |
| B | GLY99 |
| B | GLY100 |
| B | GLY101 |
| B | LYS125 |
| B | HOH491 |
| B | HOH497 |
| B | HOH517 |
| B | HOH572 |
| B | HOH685 |
| B | HOH711 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue FLC C 300 |
| Chain | Residue |
| C | THR32 |
| C | SER34 |
| C | THR35 |
| C | ALA87 |
| C | ASP88 |
| C | LYS98 |
| C | GLY99 |
| C | GLY100 |
| C | GLY101 |
| C | HOH481 |
| C | HOH533 |
| C | HOH622 |
| C | HOH661 |
| C | HOH748 |
| C | HOH749 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue FLC D 300 |
| Chain | Residue |
| D | THR32 |
| D | SER34 |
| D | THR35 |
| D | ALA87 |
| D | ASP88 |
| D | LYS98 |
| D | GLY99 |
| D | GLY100 |
| D | GLY101 |
| D | LYS125 |
| D | HOH489 |
| D | HOH508 |
| D | HOH514 |
| D | HOH526 |
| D | HOH561 |
| D | HOH586 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00170","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 40 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00170","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
