3TAO
Structure of Mycobacterium tuberculosis triosephosphate isomerase bound to phosphoglycolohydroxamate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004807 | molecular_function | triose-phosphate isomerase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019563 | biological_process | glycerol catabolic process |
| A | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
| B | 0004807 | molecular_function | triose-phosphate isomerase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006096 | biological_process | glycolytic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0019563 | biological_process | glycerol catabolic process |
| B | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PGH A 268 |
| Chain | Residue |
| A | ASN10 |
| A | SER218 |
| A | LEU237 |
| A | GLY239 |
| A | GLY240 |
| A | HOH278 |
| A | HOH317 |
| A | HOH338 |
| A | HOH414 |
| A | LYS12 |
| A | HIS100 |
| A | GLU172 |
| A | ALA176 |
| A | ILE177 |
| A | GLY178 |
| A | GLY216 |
| A | GLY217 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PGH A 269 |
| Chain | Residue |
| A | ILE21 |
| A | ARG51 |
| A | SER52 |
| A | THR55 |
| A | HOH286 |
| A | HOH400 |
| A | HOH400 |
| A | HOH756 |
| A | HOH756 |
| B | ARG51 |
| B | THR55 |
Functional Information from PROSITE/UniProt
| site_id | PS00171 |
| Number of Residues | 11 |
| Details | TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG |
| Chain | Residue | Details |
| A | ALA170-GLY180 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Electrophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00147","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22120738","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"25613812","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00147","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25613812","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00147","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22120738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25613812","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00147","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22120738","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
