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 | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00170 |
Chain | Residue | Details |
A | GLU107 | |
B | GLU107 | |
C | GLU107 | |
D | GLU107 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00170 |
Chain | Residue | Details |
A | THR32 | |
C | ASP85 | |
C | LYS98 | |
C | LYS125 | |
D | THR32 | |
D | ASP85 | |
D | LYS98 | |
D | LYS125 | |
A | ASP85 | |
A | LYS98 | |
A | LYS125 | |
B | THR32 | |
B | ASP85 | |
B | LYS98 | |
B | LYS125 | |
C | THR32 |