3E9D
Structure of full-length TIGAR from Danio rerio
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004331 | molecular_function | fructose-2,6-bisphosphate 2-phosphatase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005741 | cellular_component | mitochondrial outer membrane |
| A | 0005829 | cellular_component | cytosol |
| A | 0006914 | biological_process | autophagy |
| A | 0006915 | biological_process | apoptotic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0043456 | biological_process | regulation of pentose-phosphate shunt |
| A | 0045820 | biological_process | negative regulation of glycolytic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004331 | molecular_function | fructose-2,6-bisphosphate 2-phosphatase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0005741 | cellular_component | mitochondrial outer membrane |
| B | 0005829 | cellular_component | cytosol |
| B | 0006914 | biological_process | autophagy |
| B | 0006915 | biological_process | apoptotic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0043456 | biological_process | regulation of pentose-phosphate shunt |
| B | 0045820 | biological_process | negative regulation of glycolytic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 266 |
| Chain | Residue |
| A | ARG10 |
| A | HIS11 |
| A | ASN17 |
| A | GLN23 |
| A | ARG61 |
| A | GLU89 |
| A | HIS183 |
| A | GLY184 |
| A | HOH432 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 267 |
| Chain | Residue |
| A | ARG10 |
| A | ASN17 |
| A | ASN217 |
| A | HOH309 |
| A | HOH425 |
| A | HOH445 |
| A | HOH496 |
| A | HOH535 |
| A | HOH550 |
| A | HOH552 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 268 |
| Chain | Residue |
| A | VAL195 |
| A | GLU196 |
| A | LEU198 |
| B | LEU202 |
| B | PRO203 |
| B | HOH292 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 266 |
| Chain | Residue |
| B | ARG10 |
| B | HIS11 |
| B | ASN17 |
| B | GLN23 |
| B | ARG61 |
| B | GLU89 |
| B | HIS183 |
| B | GLY184 |
| B | HOH409 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 B 267 |
| Chain | Residue |
| B | ARG10 |
| B | ASN17 |
| B | ASN217 |
| B | HOH348 |
| B | HOH377 |
| B | HOH389 |
| B | HOH442 |
| B | HOH496 |
| B | HOH510 |
| B | HOH542 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 268 |
| Chain | Residue |
| A | LEU202 |
| A | PRO203 |
| A | HOH305 |
| B | VAL195 |
| B | GLU196 |
| B | LEU198 |
Functional Information from PROSITE/UniProt
| site_id | PS00175 |
| Number of Residues | 10 |
| Details | PG_MUTASE Phosphoglycerate mutase family phosphohistidine signature. IvRHGEtQyN |
| Chain | Residue | Details |
| A | ILE8-ASN17 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Tele-phosphohistidine intermediate => ECO:0000269|PubMed:19015259 |
| Chain | Residue | Details |
| A | HIS11 | |
| B | HIS11 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:19015259 |
| Chain | Residue | Details |
| A | GLU89 | |
| B | GLU89 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:19015259 |
| Chain | Residue | Details |
| A | HIS183 | |
| B | HIS183 |
