1R2T
CRYSTAL STRUCTURE OF RABBIT MUSCLE 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 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 |
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 |