3PWA
Structure of C126A mutant of Plasmodium falciparum triosephosphate isomerase
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE EDO A 249 |
Chain | Residue |
A | ASN10 |
A | HOH499 |
A | LYS12 |
A | HIS95 |
A | GLY209 |
A | LEU230 |
A | VAL231 |
A | GLY232 |
A | ACT250 |
A | HOH347 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACT A 250 |
Chain | Residue |
A | SER211 |
A | ASN233 |
A | EDO249 |
A | HOH289 |
B | HOH303 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 B 249 |
Chain | Residue |
B | SER211 |
B | GLY232 |
B | ASN233 |
B | HOH286 |
B | HOH288 |
B | HOH364 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ACT B 250 |
Chain | Residue |
B | GLY128 |
B | GLN133 |
B | VAL142 |
B | HOH462 |
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 | 2 |
Details | ACT_SITE: Electrophile => ECO:0000255|PROSITE-ProRule:PRU10127 |
Chain | Residue | Details |
A | HIS95 | |
B | HIS95 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU10127 |
Chain | Residue | Details |
A | GLU165 | |
B | GLU165 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
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 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
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 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
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 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
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 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
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 |