1SU5
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 | 14 |
| Details | BINDING SITE FOR RESIDUE PGA A 300 |
| Chain | Residue |
| A | LYS13 |
| A | GLY233 |
| A | HOH319 |
| A | HOH330 |
| A | HOH360 |
| A | HOH396 |
| A | HIS95 |
| A | GLU165 |
| A | ILE170 |
| A | GLY171 |
| A | GLY210 |
| A | SER211 |
| A | LEU230 |
| A | GLY232 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE PGA B 1300 |
| 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 | HOH1309 |
| B | HOH1317 |
| B | HOH1332 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 301 |
| Chain | Residue |
| A | ASP56 |
| A | ALA57 |
| A | HOH364 |
| B | LYS5 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1301 |
| Chain | Residue |
| B | SER197 |
| B | ASP198 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1302 |
| Chain | Residue |
| B | SER96 |
| B | HIS100 |
| B | VAL101 |
| B | VAL167 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 302 |
| Chain | Residue |
| A | SER197 |
| A | ASP198 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1303 |
| Chain | Residue |
| B | ALA114 |
| B | HIS115 |
| B | ALA118 |
| B | HOH1324 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1304 |
| Chain | Residue |
| A | LYS58 |
| B | LEU33 |
| B | SER34 |
| B | ALA35 |
| B | THR37 |
| B | LYS58 |
| B | HOH1361 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1305 |
| Chain | Residue |
| A | LYS5 |
| B | ASP56 |
| B | ALA57 |
| B | HOH1312 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 303 |
| Chain | Residue |
| A | ASP132 |
| A | GLU133 |
| A | ALA136 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 304 |
| Chain | Residue |
| A | LYS68 |
| A | ALA114 |
| A | HIS115 |
| A | ALA118 |
| A | HOH379 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 1 |
| Chain | Residue |
| B | LYS32 |
| B | LYS148 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 1306 |
| Chain | Residue |
| A | ASP49 |
| A | GLN53 |
| B | LYS18 |
| B | ASP49 |
| B | GLN53 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 305 |
| Chain | Residue |
| A | LYS68 |
| A | GLN111 |
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 |
