1R2R
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 |
| C | 0004807 | molecular_function | triose-phosphate isomerase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006006 | biological_process | glucose metabolic process |
| C | 0006094 | biological_process | gluconeogenesis |
| C | 0006096 | biological_process | glycolytic process |
| C | 0008929 | molecular_function | methylglyoxal synthase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0019242 | biological_process | methylglyoxal biosynthetic process |
| C | 0019563 | biological_process | glycerol catabolic process |
| C | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| C | 0031625 | molecular_function | ubiquitin protein ligase binding |
| C | 0042803 | molecular_function | protein homodimerization activity |
| C | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
| C | 0061621 | biological_process | canonical glycolysis |
| D | 0004807 | molecular_function | triose-phosphate isomerase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006006 | biological_process | glucose metabolic process |
| D | 0006094 | biological_process | gluconeogenesis |
| D | 0006096 | biological_process | glycolytic process |
| D | 0008929 | molecular_function | methylglyoxal synthase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0019242 | biological_process | methylglyoxal biosynthetic process |
| D | 0019563 | biological_process | glycerol catabolic process |
| D | 0019682 | biological_process | glyceraldehyde-3-phosphate metabolic process |
| D | 0031625 | molecular_function | ubiquitin protein ligase binding |
| D | 0042803 | molecular_function | protein homodimerization activity |
| D | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
| D | 0061621 | biological_process | canonical glycolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS A 249 |
| Chain | Residue |
| A | THR89 |
| A | TRP90 |
| A | GLY122 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DMS A 253 |
| Chain | Residue |
| A | LYS218 |
| A | SER222 |
| A | ALA246 |
| A | LYS247 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS A 255 |
| Chain | Residue |
| A | HOH545 |
| D | GLU135 |
| D | ALA136 |
| A | LYS68 |
| A | HOH311 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 257 |
| Chain | Residue |
| B | ARG99 |
| B | ASP106 |
| B | GLN146 |
| B | HOH538 |
| B | HOH822 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS B 249 |
| Chain | Residue |
| B | THR89 |
| B | TRP90 |
| B | GLY120 |
| B | GLY122 |
| B | LYS159 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE DMS B 250 |
| Chain | Residue |
| B | ASN20 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS B 252 |
| Chain | Residue |
| B | ARG134 |
| B | GLU183 |
| B | LYS187 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DMS B 255 |
| Chain | Residue |
| A | GLY103 |
| A | LEU108 |
| A | HOH515 |
| A | HOH543 |
| B | VAL101 |
| D | LYS141 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS B 256 |
| Chain | Residue |
| B | SER197 |
| B | ASP198 |
| B | HOH613 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 261 |
| Chain | Residue |
| B | HOH838 |
| B | HOH840 |
| B | HOH1156 |
| C | HOH832 |
| C | HOH834 |
| C | HOH836 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 260 |
| Chain | Residue |
| C | HOH540 |
| C | HOH542 |
| C | HOH824 |
| C | HOH826 |
| C | HOH828 |
| C | HOH830 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 263 |
| Chain | Residue |
| C | HOH846 |
| C | HOH848 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG C 262 |
| Chain | Residue |
| C | SER96 |
| C | HOH842 |
| C | HOH844 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DMS C 249 |
| Chain | Residue |
| C | THR89 |
| C | TRP90 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DMS C 250 |
| Chain | Residue |
| C | ASN20 |
| C | HOH1051 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DMS C 251 |
| Chain | Residue |
| C | GLY16 |
| C | ARG17 |
| C | ASN20 |
| C | HOH971 |
| C | HOH1051 |
| C | HOH1097 |
| D | ASN71 |
| D | TRS258 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DMS C 254 |
| Chain | Residue |
| A | SER194 |
| A | HOH492 |
| B | GLU186 |
| C | ASP132 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS C 257 |
| Chain | Residue |
| C | LYS130 |
| C | LEU131 |
| C | VAL167 |
| C | HOH880 |
| C | HOH889 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DMS D 254 |
| Chain | Residue |
| B | ALA136 |
| C | HOH975 |
| C | HOH1104 |
| C | HOH1114 |
| D | VAL101 |
| D | PHE102 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS D 258 |
| Chain | Residue |
| C | TRP191 |
| C | ASN195 |
| C | DMS251 |
| C | HOH881 |
| C | HOH1035 |
| D | ASN71 |
| D | HOH1267 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE TRS C 259 |
| Chain | Residue |
| C | VAL149 |
| C | ASP152 |
| C | ASN153 |
| C | LYS237 |
| C | HOH960 |
| site_id | CC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG D 249 |
| Chain | Residue |
| B | HOH835 |
| B | HOH1160 |
| B | HOH1166 |
| D | HOH850 |
| D | HOH1158 |
| D | HOH1162 |
| D | HOH1164 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 255 |
| Chain | Residue |
| D | TRP191 |
| D | HOH852 |
| D | HOH854 |
| D | HOH1172 |
| D | PHE144 |
| site_id | CC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 256 |
| Chain | Residue |
| D | ASP156 |
| D | THR177 |
| D | HOH544 |
| D | HOH546 |
| D | HOH1386 |
| site_id | CC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 257 |
| Chain | Residue |
| D | SER96 |
| D | HOH856 |
| D | HOH1168 |
| site_id | CC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS D 250 |
| Chain | Residue |
| D | ASN20 |
| D | LEU21 |
| D | LEU236 |
| site_id | CC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE DMS D 252 |
| Chain | Residue |
| D | ARG134 |
| D | THR139 |
| D | GLU183 |
| D | VAL184 |
| D | LYS187 |
| D | HOH1195 |
| D | HOH1349 |
| site_id | DC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS D 253 |
| Chain | Residue |
| C | SER222 |
| C | PRO224 |
| D | SER222 |
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 | 4 |
| Details | ACT_SITE: Electrophile => ECO:0000255|PROSITE-ProRule:PRU10127 |
| Chain | Residue | Details |
| A | SER96 | |
| B | SER96 | |
| C | SER96 | |
| D | SER96 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:4922541 |
| Chain | Residue | Details |
| A | PRO166 | |
| B | PRO166 | |
| C | PRO166 | |
| D | PRO166 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU10127 |
| Chain | Residue | Details |
| A | TRP12 | |
| A | MET14 | |
| B | TRP12 | |
| B | MET14 | |
| C | TRP12 | |
| C | MET14 | |
| D | TRP12 | |
| D | MET14 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P60174 |
| Chain | Residue | Details |
| A | MET14 | |
| A | PRO238 | |
| B | MET14 | |
| B | PRO238 | |
| C | MET14 | |
| C | PRO238 | |
| D | MET14 | |
| D | PRO238 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: Deamidated asparagine => ECO:0000269|PubMed:7574709 |
| Chain | Residue | Details |
| A | GLY16 | |
| A | GLY72 | |
| B | GLY16 | |
| B | GLY72 | |
| C | GLY16 | |
| C | GLY72 | |
| D | GLY16 | |
| D | GLY72 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: 3'-nitrotyrosine => ECO:0000250|UniProtKB:P17751 |
| Chain | Residue | Details |
| A | LYS68 | |
| A | GLY209 | |
| B | LYS68 | |
| B | GLY209 | |
| C | LYS68 | |
| C | GLY209 | |
| D | LYS68 | |
| D | GLY209 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P60174 |
| Chain | Residue | Details |
| A | PRO80 | |
| D | PRO80 | |
| D | VAL212 | |
| D | GLN223 | |
| A | VAL212 | |
| A | GLN223 | |
| B | PRO80 | |
| B | VAL212 | |
| B | GLN223 | |
| C | PRO80 | |
| C | VAL212 | |
| C | GLN223 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P48500 |
| Chain | Residue | Details |
| A | ASP106 | |
| A | ASP198 | |
| B | ASP106 | |
| B | ASP198 | |
| C | ASP106 | |
| C | ASP198 | |
| D | ASP106 | |
| D | ASP198 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P17751 |
| Chain | Residue | Details |
| A | VAL149 | |
| B | VAL149 | |
| C | VAL149 | |
| D | VAL149 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17751 |
| Chain | Residue | Details |
| A | ASP156 | |
| A | SER194 | |
| B | ASP156 | |
| B | SER194 | |
| C | ASP156 | |
| C | SER194 | |
| D | ASP156 | |
| D | SER194 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P17751 |
| Chain | Residue | Details |
| A | LYS159 | |
| B | LYS159 | |
| C | LYS159 | |
| D | LYS159 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P17751 |
| Chain | Residue | Details |
| A | GLY173 | |
| B | GLY173 | |
| C | GLY173 | |
| D | GLY173 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P60174 |
| Chain | Residue | Details |
| A | GLY214 | |
| B | GLY214 | |
| C | GLY214 | |
| D | GLY214 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0000250|UniProtKB:P60174 |
| Chain | Residue | Details |
| A | VAL142 | |
| B | VAL142 | |
| C | VAL142 | |
| D | 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 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1hti |
| Chain | Residue | Details |
| C | LYS13 | |
| C | HIS95 | |
| C | ASN11 | |
| C | GLU165 | |
| C | GLY171 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1hti |
| Chain | Residue | Details |
| D | LYS13 | |
| D | HIS95 | |
| D | ASN11 | |
| D | GLU165 | |
| D | GLY171 |
