5BMX
Crystal structure of T75N mutant of Triosephosphate isomerase from Plasmodium falciparum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004807 | molecular_function | triose-phosphate isomerase activity |
| 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 | 0042802 | molecular_function | identical protein binding |
| A | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
| B | 0004807 | molecular_function | triose-phosphate isomerase activity |
| 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 | 0042802 | molecular_function | identical protein binding |
| B | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
| C | 0004807 | molecular_function | triose-phosphate isomerase activity |
| 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 | 0042802 | molecular_function | identical protein binding |
| C | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
| D | 0004807 | molecular_function | triose-phosphate isomerase activity |
| 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 | 0042802 | molecular_function | identical protein binding |
| D | 0046166 | biological_process | glyceraldehyde-3-phosphate biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 301 |
| Chain | Residue |
| A | ASN10 |
| A | LYS12 |
| A | HIS95 |
| A | LEU230 |
| A | HOH413 |
| A | HOH444 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | LYS36 |
| A | ARG3 |
| A | LYS4 |
| A | TYR5 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 303 |
| Chain | Residue |
| A | ILE221 |
| A | GLN223 |
| A | ILE226 |
| A | HOH430 |
| A | HOH474 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 304 |
| Chain | Residue |
| A | SER211 |
| A | GLY232 |
| A | ASN233 |
| A | HOH415 |
| A | HOH426 |
| A | HOH547 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 301 |
| Chain | Residue |
| B | ASN65 |
| B | HOH420 |
| B | HOH479 |
| B | HOH526 |
| B | HOH557 |
| B | HOH565 |
| C | GLY76 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | GLY76 |
| B | HOH447 |
| B | HOH460 |
| B | HOH512 |
| C | ASN65 |
| C | HOH487 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| B | ASN10 |
| B | LYS12 |
| B | HIS95 |
| B | LEU230 |
| B | HOH468 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 304 |
| Chain | Residue |
| B | TYR5 |
| B | ILE221 |
| B | GLN223 |
| B | ILE226 |
| B | HOH506 |
| B | HOH555 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 305 |
| Chain | Residue |
| B | SER211 |
| B | GLY232 |
| B | ASN233 |
| B | HOH402 |
| B | HOH404 |
| B | HOH422 |
| B | HOH554 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 301 |
| Chain | Residue |
| C | ASN10 |
| C | LYS12 |
| C | HIS95 |
| C | LEU230 |
| C | SO4303 |
| C | HOH411 |
| C | HOH438 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 302 |
| Chain | Residue |
| C | TYR5 |
| C | ILE221 |
| C | GLN223 |
| C | ILE226 |
| C | HOH491 |
| C | HOH524 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 303 |
| Chain | Residue |
| C | SER211 |
| C | ASN233 |
| C | EDO301 |
| C | HOH402 |
| C | HOH463 |
| C | HOH561 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO D 301 |
| Chain | Residue |
| A | GLY76 |
| A | HOH482 |
| D | ASN65 |
| D | HOH417 |
| D | HOH457 |
| D | HOH482 |
| D | HOH501 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue EDO D 302 |
| Chain | Residue |
| D | ASN10 |
| D | LYS12 |
| D | HIS95 |
| D | LEU230 |
| D | GLY232 |
| D | SO4304 |
| D | HOH416 |
| D | HOH438 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue NA D 303 |
| Chain | Residue |
| D | TYR5 |
| D | ILE221 |
| D | GLN223 |
| D | ILE226 |
| D | HOH500 |
| D | HOH535 |
| site_id | AD7 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 D 304 |
| Chain | Residue |
| D | SER211 |
| D | GLY232 |
| D | ASN233 |
| D | EDO302 |
| D | HOH420 |
| D | HOH433 |
| D | HOH441 |
Functional Information from PROSITE/UniProt
| site_id | PS00171 |
| Number of Residues | 11 |
| Details | TIM_1 Triosephosphate isomerase active site. VYEPLWAIGTG |
| Chain | Residue | Details |
| A | VAL163-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 | HIS95 | |
| B | HIS95 | |
| C | HIS95 | |
| D | HIS95 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10127 |
| Chain | Residue | Details |
| A | GLU165 | |
| B | GLU165 | |
| C | GLU165 | |
| D | GLU165 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12454456, ECO:0000269|PubMed:14563846, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1M7O, ECO:0007744|PDB:1O5X, ECO:0007744|PDB:2VFI |
| Chain | Residue | Details |
| A | ASN10 | |
| B | ASN10 | |
| C | ASN10 | |
| D | ASN10 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12403619, ECO:0000269|PubMed:15465054, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1LYX, ECO:0007744|PDB:1LZO, ECO:0007744|PDB:1WOA, ECO:0007744|PDB:2VFI |
| Chain | Residue | Details |
| A | LYS12 | |
| B | LYS12 | |
| C | LYS12 | |
| D | LYS12 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12403619, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1LYX, ECO:0007744|PDB:2VFI |
| Chain | Residue | Details |
| A | GLY171 | |
| B | GLY171 | |
| C | GLY171 | |
| D | GLY171 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12454456, ECO:0000269|PubMed:14563846, ECO:0000269|PubMed:15465054, ECO:0000269|PubMed:19622869, ECO:0007744|PDB:1M7O, ECO:0007744|PDB:1O5X, ECO:0007744|PDB:1WOA, ECO:0007744|PDB:2VFI |
| Chain | Residue | Details |
| A | LEU230 | |
| B | LEU230 | |
| C | LEU230 | |
| D | LEU230 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12403619, ECO:0000269|PubMed:12454456, ECO:0000269|PubMed:14563846, ECO:0000269|PubMed:15465054, ECO:0000269|PubMed:19622869, ECO:0000312|PDB:1LZO, ECO:0007744|PDB:1LYX, ECO:0007744|PDB:1M7O, ECO:0007744|PDB:1M7P, ECO:0007744|PDB:1O5X, ECO:0007744|PDB:1WOA, ECO:0007744|PDB:2VFI |
| Chain | Residue | Details |
| A | GLY232 | |
| B | GLY232 | |
| C | GLY232 | |
| D | GLY232 |
