1SSG
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 | 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 | 12 |
Details | BINDING SITE FOR RESIDUE PGA A 300 |
Chain | Residue |
A | ASN11 |
A | GLY232 |
A | GLY233 |
A | HOH351 |
A | LYS13 |
A | HIS95 |
A | GLU165 |
A | ALA169 |
A | ILE170 |
A | GLY171 |
A | GLY210 |
A | SER211 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PGA B 1300 |
Chain | Residue |
B | ASN11 |
B | LYS13 |
B | HIS95 |
B | GLU165 |
B | ALA169 |
B | ILE170 |
B | GLY171 |
B | SER211 |
B | LEU230 |
B | GLY232 |
B | GLY233 |
B | HOH1312 |
B | HOH1337 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 1301 |
Chain | Residue |
B | HIS100 |
B | LYS130 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 1302 |
Chain | Residue |
A | LYS5 |
B | ASP56 |
B | ALA57 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE SO4 A 301 |
Chain | Residue |
A | THR213 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 302 |
Chain | Residue |
A | ARG99 |
A | HIS100 |
A | LYS130 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 1 |
Chain | Residue |
A | PHE50 |
A | GLN53 |
A | HOH340 |
B | ASP49 |
B | PHE50 |
B | GLN53 |
site_id | AC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 1303 |
Chain | Residue |
B | LYS68 |
B | ALA114 |
B | HIS115 |
B | ALA118 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL B 1304 |
Chain | Residue |
B | SER197 |
B | ASP198 |
B | HOH1343 |
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 | ACT_SITE: Electrophile => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH |
Chain | Residue | Details |
A | SER96 | |
B | SER96 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH |
Chain | Residue | Details |
A | PRO166 | |
B | PRO166 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8130195, ECO:0007744|PDB:1TPH |
Chain | Residue | Details |
A | TRP12 | |
A | MET14 | |
B | TRP12 | |
B | MET14 |
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 | TRP12 | electrostatic stabiliser |
A | MET14 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | SER96 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | ARG98 | proton acceptor, proton donor, steric role |
A | PRO166 | activator, proton acceptor, proton donor |
A | THR172 | electrostatic stabiliser |
A | VAL212 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 7 |
Details | M-CSA 324 |
Chain | Residue | Details |
B | TRP12 | electrostatic stabiliser |
B | MET14 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | SER96 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | ARG98 | proton acceptor, proton donor, steric role |
B | PRO166 | activator, proton acceptor, proton donor |
B | THR172 | electrostatic stabiliser |
B | VAL212 | electrostatic stabiliser, hydrogen bond donor |