4Y90
Crystal structure of Triosephosphate Isomerase from Deinococcus radiodurans
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 | 0016853 | molecular_function | isomerase activity |
| A | 0019563 | biological_process | glycerol catabolic process |
| A | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
| 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 | 0016853 | molecular_function | isomerase activity |
| B | 0019563 | biological_process | glycerol catabolic process |
| B | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
| C | 0004807 | molecular_function | triose-phosphate isomerase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006094 | biological_process | gluconeogenesis |
| C | 0006096 | biological_process | glycolytic process |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0019563 | biological_process | glycerol catabolic process |
| C | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
| D | 0004807 | molecular_function | triose-phosphate isomerase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006094 | biological_process | gluconeogenesis |
| D | 0006096 | biological_process | glycolytic process |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0019563 | biological_process | glycerol catabolic process |
| D | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 301 |
| Chain | Residue |
| A | ILE169 |
| A | GLY170 |
| A | SER209 |
| A | GLY230 |
| A | GLY231 |
| A | HOH470 |
| A | HOH491 |
| A | HOH493 |
| A | HOH526 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 302 |
| Chain | Residue |
| A | HIS70 |
| A | GLU71 |
| A | SER72 |
| A | GLN116 |
| C | HOH403 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 303 |
| Chain | Residue |
| A | GLU182 |
| A | HOH409 |
| A | HOH414 |
| B | GLU71 |
| B | GLN116 |
| B | HOH445 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 304 |
| Chain | Residue |
| A | HOH402 |
| A | HOH404 |
| B | GLU193 |
| B | GLN194 |
| B | ARG198 |
| B | GOL305 |
| B | HOH432 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue CA A 305 |
| Chain | Residue |
| A | ASN11 |
| A | LYS13 |
| A | HIS96 |
| A | GLU164 |
| A | HOH523 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | binding site for residue SO4 B 301 |
| Chain | Residue |
| B | ALA168 |
| B | ILE169 |
| B | GLY170 |
| B | SER209 |
| B | GLY230 |
| B | GLY231 |
| B | HOH464 |
| B | HOH496 |
| B | HOH507 |
| B | HOH583 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 302 |
| Chain | Residue |
| A | HOH409 |
| A | HOH420 |
| B | HIS70 |
| B | GLU71 |
| B | SER72 |
| B | HOH542 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 303 |
| Chain | Residue |
| A | GLY77 |
| B | ASP66 |
| B | GLU78 |
| B | ILE79 |
| B | HOH456 |
| B | HOH597 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 304 |
| Chain | Residue |
| B | PRO34 |
| B | ALA35 |
| B | GLU36 |
| B | ARG247 |
| B | HOH417 |
| B | HOH426 |
| D | THR30 |
| D | LYS31 |
| D | TYR32 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL B 305 |
| Chain | Residue |
| A | GOL304 |
| B | TYR195 |
| B | GLY196 |
| B | ALA197 |
| B | ARG198 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue CA B 306 |
| Chain | Residue |
| B | ASN11 |
| B | HIS96 |
| B | GLU164 |
| B | HOH514 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue CA B 307 |
| Chain | Residue |
| B | CYS219 |
| B | LYS221 |
| B | VAL224 |
| B | HOH601 |
| site_id | AD4 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 C 301 |
| Chain | Residue |
| C | GLY170 |
| C | SER209 |
| C | GLY230 |
| C | GLY231 |
| C | HOH494 |
| C | HOH497 |
| C | HOH500 |
| C | HOH518 |
| C | HOH529 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 302 |
| Chain | Residue |
| C | ASP66 |
| C | GLU78 |
| C | ILE79 |
| C | CA306 |
| C | HOH447 |
| D | GLY77 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 303 |
| Chain | Residue |
| B | ARG135 |
| C | HIS70 |
| C | GLU71 |
| C | SER72 |
| C | HOH413 |
| C | HOH547 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue NA C 304 |
| Chain | Residue |
| C | GLU164 |
| C | HOH497 |
| C | ASN11 |
| C | HIS96 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue NA C 305 |
| Chain | Residue |
| C | CYS219 |
| C | LYS221 |
| C | VAL224 |
| C | HOH577 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue CA C 306 |
| Chain | Residue |
| C | ASP66 |
| C | LYS113 |
| C | GOL302 |
| D | HIS103 |
| site_id | AE1 |
| Number of Residues | 11 |
| Details | binding site for residue SO4 D 301 |
| Chain | Residue |
| D | LYS13 |
| D | ALA168 |
| D | GLY170 |
| D | SER209 |
| D | GLY230 |
| D | GLY231 |
| D | CA304 |
| D | HOH518 |
| D | HOH520 |
| D | HOH531 |
| D | HOH588 |
| site_id | AE2 |
| Number of Residues | 5 |
| Details | binding site for residue GOL D 302 |
| Chain | Residue |
| D | HIS70 |
| D | GLU71 |
| D | HIS140 |
| D | HOH426 |
| D | HOH576 |
| site_id | AE3 |
| Number of Residues | 3 |
| Details | binding site for residue NA D 303 |
| Chain | Residue |
| D | ASN11 |
| D | HIS96 |
| D | GLU164 |
| site_id | AE4 |
| Number of Residues | 7 |
| Details | binding site for residue CA D 304 |
| Chain | Residue |
| D | GLY208 |
| D | SER209 |
| D | VAL210 |
| D | LEU228 |
| D | VAL229 |
| D | GLY230 |
| D | SO4301 |
Functional Information from PROSITE/UniProt
| site_id | PS00171 |
| Number of Residues | 11 |
| Details | TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG |
| Chain | Residue | Details |
| A | ALA162-GLY172 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Electrophile => ECO:0000255|HAMAP-Rule:MF_00147 |
| Chain | Residue | Details |
| A | HIS96 | |
| B | HIS96 | |
| C | HIS96 | |
| D | HIS96 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00147 |
| Chain | Residue | Details |
| A | GLU164 | |
| B | GLU164 | |
| C | GLU164 | |
| D | GLU164 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00147 |
| Chain | Residue | Details |
| A | ASN11 | |
| C | GLY170 | |
| C | SER209 | |
| C | GLY230 | |
| D | ASN11 | |
| D | GLY170 | |
| D | SER209 | |
| D | GLY230 | |
| A | GLY170 | |
| A | SER209 | |
| A | GLY230 | |
| B | ASN11 | |
| B | GLY170 | |
| B | SER209 | |
| B | GLY230 | |
| C | ASN11 |
