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 | 0016310 | biological_process | phosphorylation |
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 | 0016310 | biological_process | phosphorylation |
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 |