1SPQ
Understanding protein lids: Structural analysis of active hinge mutants in triosephosphate isomerase
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 | 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 | 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 | 5 |
| Details | BINDING SITE FOR RESIDUE PEG B 1001 |
| Chain | Residue |
| A | ASN15 |
| A | SER222 |
| B | LYS71 |
| B | HOH1159 |
| B | HOH1162 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG B 1002 |
| Chain | Residue |
| B | GLN53 |
| B | HOH1146 |
| B | HOH1156 |
| A | ASP49 |
| A | GLN53 |
| B | LYS18 |
| B | ASP49 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PEG A 1003 |
| Chain | Residue |
| A | PHE102 |
| B | VAL101 |
| B | PHE102 |
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 | GLY173 | |
| A | GLU165 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1hti |
| Chain | Residue | Details |
| B | LYS13 | |
| B | HIS95 | |
| B | ASN11 | |
| B | GLU165 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| 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 | SER211 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| 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 | SER211 | electrostatic stabiliser, hydrogen bond donor |
