4OWG
Crystal structure of rabbit muscle triosephosphate isomerase-PEP complex
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 | 16 |
| Details | binding site for residue PEP A 301 |
| Chain | Residue |
| A | ASN11 |
| A | LEU230 |
| A | GLY232 |
| A | GLY233 |
| A | HOH419 |
| A | HOH512 |
| A | HOH516 |
| A | HOH524 |
| A | LYS13 |
| A | HIS95 |
| A | GLU165 |
| A | ALA169 |
| A | ILE170 |
| A | GLY171 |
| A | GLY210 |
| A | SER211 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue PEP B 301 |
| Chain | Residue |
| B | ASN11 |
| B | LYS13 |
| B | HIS95 |
| B | GLU165 |
| B | ALA169 |
| B | ILE170 |
| B | GLY171 |
| B | GLY209 |
| B | GLY210 |
| B | SER211 |
| B | GLY232 |
| B | GLY233 |
| B | HOH406 |
| B | HOH467 |
| B | HOH472 |
| B | HOH499 |
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:0000255|PROSITE-ProRule:PRU10127 |
| Chain | Residue | Details |
| A | SER96 | |
| B | SER96 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:4922541 |
| Chain | Residue | Details |
| A | PRO166 | |
| B | PRO166 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10127 |
| Chain | Residue | Details |
| A | TRP12 | |
| A | MET14 | |
| B | TRP12 | |
| B | MET14 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P60174 |
| Chain | Residue | Details |
| A | MET14 | |
| A | PRO238 | |
| B | MET14 | |
| B | PRO238 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Deamidated asparagine => ECO:0000269|PubMed:7574709 |
| Chain | Residue | Details |
| A | GLY16 | |
| A | GLY72 | |
| B | GLY16 | |
| B | GLY72 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P17751 |
| Chain | Residue | Details |
| A | LYS68 | |
| A | GLY209 | |
| B | LYS68 | |
| B | GLY209 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P60174 |
| Chain | Residue | Details |
| A | PRO80 | |
| A | VAL212 | |
| A | GLN223 | |
| B | PRO80 | |
| B | VAL212 | |
| B | GLN223 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48500 |
| Chain | Residue | Details |
| A | ASP106 | |
| A | ASP198 | |
| B | ASP106 | |
| B | ASP198 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P17751 |
| Chain | Residue | Details |
| A | VAL149 | |
| B | VAL149 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17751 |
| Chain | Residue | Details |
| A | ASP156 | |
| A | SER194 | |
| B | ASP156 | |
| B | SER194 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P17751 |
| Chain | Residue | Details |
| A | LYS159 | |
| B | LYS159 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17751 |
| Chain | Residue | Details |
| A | GLY173 | |
| B | GLY173 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P60174 |
| Chain | Residue | Details |
| A | GLY214 | |
| B | GLY214 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000250|UniProtKB:P60174 |
| Chain | Residue | Details |
| A | VAL142 | |
| B | VAL142 |
