1UN9
Crystal structure of the dihydroxyacetone kinase from C. freundii in complex with AMP-PNP and Mg2+
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004371 | molecular_function | glycerone kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006071 | biological_process | glycerol metabolic process |
| A | 0008289 | molecular_function | lipid binding |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| A | 0019563 | biological_process | glycerol catabolic process |
| A | 0019588 | biological_process | anaerobic glycerol catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0004371 | molecular_function | glycerone kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006071 | biological_process | glycerol metabolic process |
| B | 0008289 | molecular_function | lipid binding |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016773 | molecular_function | phosphotransferase activity, alcohol group as acceptor |
| B | 0019563 | biological_process | glycerol catabolic process |
| B | 0019588 | biological_process | anaerobic glycerol catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A1552 |
| Chain | Residue |
| A | ASP380 |
| A | ASP385 |
| A | ASP387 |
| A | ANP1551 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A1553 |
| Chain | Residue |
| A | ASP385 |
| A | ASP387 |
| A | ANP1551 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B1552 |
| Chain | Residue |
| B | ASP387 |
| B | ANP1551 |
| B | ASP380 |
| B | ASP385 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B1553 |
| Chain | Residue |
| B | ASP385 |
| B | ASP387 |
| B | ANP1551 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE ANP A1551 |
| Chain | Residue |
| A | ASP385 |
| A | ASP387 |
| A | THR388 |
| A | THR391 |
| A | GLY430 |
| A | SER431 |
| A | SER432 |
| A | LEU435 |
| A | GLY468 |
| A | ALA470 |
| A | THR476 |
| A | MET477 |
| A | ASP533 |
| A | GLY535 |
| A | MG1552 |
| A | MG1553 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 2HA A1554 |
| Chain | Residue |
| A | GLY57 |
| A | GLY58 |
| A | HIS61 |
| A | PHE83 |
| A | ALA84 |
| A | LYS109 |
| A | ASP114 |
| A | HIS220 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ANP B1551 |
| Chain | Residue |
| B | ASP380 |
| B | ASP385 |
| B | ASP387 |
| B | THR388 |
| B | GLY430 |
| B | SER431 |
| B | SER432 |
| B | LEU435 |
| B | MET464 |
| B | GLY468 |
| B | ALA470 |
| B | THR476 |
| B | MET477 |
| B | ILE478 |
| B | ASP533 |
| B | PRO534 |
| B | GLY535 |
| B | MG1552 |
| B | MG1553 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 2HA B1554 |
| Chain | Residue |
| B | GLY57 |
| B | GLY58 |
| B | HIS61 |
| B | PHE83 |
| B | LYS109 |
| B | ASP114 |
| B | HIS220 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Tele-hemiaminal-histidine intermediate => ECO:0000255|PROSITE-ProRule:PRU00814, ECO:0000269|PubMed:12966101 |
| Chain | Residue | Details |
| A | HIS220 | |
| B | HIS220 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY58 | |
| A | LYS109 | |
| A | ASP114 | |
| B | GLY58 | |
| B | LYS109 | |
| B | ASP114 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12966101 |
| Chain | Residue | Details |
| A | ASP385 | |
| B | ASP533 | |
| A | SER431 | |
| A | GLY468 | |
| A | THR476 | |
| A | ASP533 | |
| B | ASP385 | |
| B | SER431 | |
| B | GLY468 | |
| B | THR476 |
