4DA5
Choline Kinase alpha acts through a double-displacement kinetic mechanism involving enzyme isomerisation, as determined through enzyme and inhibitor kinetics and structural biology
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004103 | molecular_function | choline kinase activity |
| A | 0004104 | molecular_function | cholinesterase activity |
| A | 0004305 | molecular_function | ethanolamine kinase activity |
| A | 0004713 | molecular_function | protein tyrosine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005811 | cellular_component | lipid droplet |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006646 | biological_process | phosphatidylethanolamine biosynthetic process |
| A | 0006656 | biological_process | phosphatidylcholine biosynthetic process |
| A | 0006657 | biological_process | CDP-choline pathway |
| A | 0006869 | biological_process | lipid transport |
| A | 0008654 | biological_process | phospholipid biosynthetic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| B | 0004103 | molecular_function | choline kinase activity |
| B | 0004104 | molecular_function | cholinesterase activity |
| B | 0004305 | molecular_function | ethanolamine kinase activity |
| B | 0004713 | molecular_function | protein tyrosine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005811 | cellular_component | lipid droplet |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006646 | biological_process | phosphatidylethanolamine biosynthetic process |
| B | 0006656 | biological_process | phosphatidylcholine biosynthetic process |
| B | 0006657 | biological_process | CDP-choline pathway |
| B | 0006869 | biological_process | lipid transport |
| B | 0008654 | biological_process | phospholipid biosynthetic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 501 |
| Chain | Residue |
| A | ARG270 |
| A | TYR359 |
| A | PHE435 |
| A | GLY436 |
| A | TYR437 |
| A | MET438 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 0H7 A 502 |
| Chain | Residue |
| A | TYR354 |
| A | TRP420 |
| A | TRP423 |
| A | PHE435 |
| A | TYR437 |
| A | TYR440 |
| A | HOH693 |
| A | ASP306 |
| A | GLN308 |
| A | GLU349 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 B 501 |
| Chain | Residue |
| B | ARG270 |
| B | LYS273 |
| B | TYR359 |
| B | GLY436 |
| B | TYR437 |
| B | MET438 |
| B | ASP439 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 0H7 B 502 |
| Chain | Residue |
| B | ASP306 |
| B | GLN308 |
| B | GLU349 |
| B | TYR354 |
| B | TRP420 |
| B | TRP423 |
| B | ILE433 |
| B | PHE435 |
| B | TYR437 |
| B | TYR440 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17007874, ECO:0000269|PubMed:20299452, ECO:0007744|PDB:2CKP, ECO:0007744|PDB:3G15 |
| Chain | Residue | Details |
| A | ARG117 | |
| A | ARG146 | |
| A | GLN207 | |
| A | ASP330 | |
| B | ARG117 | |
| B | ARG146 | |
| B | GLN207 | |
| B | ASP330 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17007874, ECO:0007744|PDB:2CKQ |
| Chain | Residue | Details |
| A | GLY119 | |
| B | GLY119 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | GLN308 | |
| B | GLN308 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:34077757 |
| Chain | Residue | Details |
| A | LYS247 | |
| B | LYS247 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:34077757 |
| Chain | Residue | Details |
| A | SER279 | |
| B | SER279 |
