3UWY
Crystal structure of triosephosphate isomerase from Methicillin resistant Staphylococcus Aureus at 2.4 angstrom resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004807 | molecular_function | triose-phosphate isomerase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0006094 | biological_process | gluconeogenesis |
A | 0006096 | biological_process | glycolytic process |
A | 0016853 | molecular_function | isomerase activity |
B | 0004807 | molecular_function | triose-phosphate isomerase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006094 | biological_process | gluconeogenesis |
B | 0006096 | biological_process | glycolytic process |
B | 0016853 | molecular_function | isomerase activity |
Functional Information from PROSITE/UniProt
site_id | PS00171 |
Number of Residues | 11 |
Details | TIM_1 Triosephosphate isomerase active site. AYEPIWAIGTG |
Chain | Residue | Details |
A | ALA167-GLY177 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Electrophile => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000305|PubMed:22813930 |
Chain | Residue | Details |
A | HIS97 | |
B | HIS97 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000305|PubMed:22813930 |
Chain | Residue | Details |
A | GLU169 | |
B | GLU169 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:22813930 |
Chain | Residue | Details |
A | ASN9 | |
A | GLY175 | |
A | SER215 | |
A | GLY236 | |
B | ASN9 | |
B | GLY175 | |
B | SER215 | |
B | GLY236 |