1SW7
Triosephosphate isomerase from Gallus gallus, loop 6 mutant K174N, T175S, A176S
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004807 | molecular_function | triose-phosphate isomerase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006094 | biological_process | gluconeogenesis |
| A | 0006096 | biological_process | glycolytic process |
| A | 0008929 | molecular_function | methylglyoxal synthase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0019242 | biological_process | methylglyoxal biosynthetic process |
| A | 0019563 | biological_process | glycerol catabolic process |
| A | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| A | 0031625 | molecular_function | ubiquitin protein ligase binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
| A | 0061621 | biological_process | canonical glycolysis |
| B | 0004807 | molecular_function | triose-phosphate isomerase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006006 | biological_process | glucose metabolic process |
| B | 0006094 | biological_process | gluconeogenesis |
| B | 0006096 | biological_process | glycolytic process |
| B | 0008929 | molecular_function | methylglyoxal synthase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0019242 | biological_process | methylglyoxal biosynthetic process |
| B | 0019563 | biological_process | glycerol catabolic process |
| B | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| B | 0031625 | molecular_function | ubiquitin protein ligase binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
| B | 0061621 | biological_process | canonical glycolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PGA A 1350 |
| Chain | Residue |
| A | LYS13 |
| A | GLY232 |
| A | GLY233 |
| A | HOH1352 |
| A | HOH1397 |
| A | HOH1421 |
| A | HOH1463 |
| A | HIS95 |
| A | GLU165 |
| A | ALA169 |
| A | ILE170 |
| A | GLY171 |
| A | GLY210 |
| A | SER211 |
| A | LEU230 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PGA B 2350 |
| Chain | Residue |
| B | LYS13 |
| B | HIS95 |
| B | GLU165 |
| B | ALA169 |
| B | ILE170 |
| B | GLY171 |
| B | GLY210 |
| B | SER211 |
| B | LEU230 |
| B | GLY232 |
| B | GLY233 |
| B | HOH2370 |
| B | HOH2391 |
| B | HOH2405 |
| B | HOH2470 |
Functional Information from PROSITE/UniProt
| site_id | PS00171 |
| Number of Residues | 11 |
| Details | TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG |
| Chain | Residue | Details |
| A | ALA163-GLY173 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Electrophile","evidences":[{"source":"PubMed","id":"8130195","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TPH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"8130195","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TPH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8130195","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TPH","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1hti |
| Chain | Residue | Details |
| A | LYS13 | |
| A | HIS95 | |
| A | ASN11 | |
| A | GLU165 | |
| A | GLY171 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1hti |
| Chain | Residue | Details |
| B | LYS13 | |
| B | HIS95 | |
| B | ASN11 | |
| B | GLU165 | |
| B | GLY171 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 324 |
| Chain | Residue | Details |
| A | ASN11 | electrostatic stabiliser |
| A | LYS13 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| A | HIS95 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU97 | proton acceptor, proton donor, steric role |
| A | GLU165 | activator, proton acceptor, proton donor |
| A | GLY171 | electrostatic stabiliser |
| A | SER211 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 324 |
| Chain | Residue | Details |
| B | ASN11 | electrostatic stabiliser |
| B | LYS13 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
| B | HIS95 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | GLU97 | proton acceptor, proton donor, steric role |
| B | GLU165 | activator, proton acceptor, proton donor |
| B | GLY171 | electrostatic stabiliser |
| B | SER211 | electrostatic stabiliser, hydrogen bond donor |
