2IG7
Crystal structure of Human Choline Kinase B
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004103 | molecular_function | choline kinase activity |
| A | 0004305 | molecular_function | ethanolamine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006646 | biological_process | phosphatidylethanolamine biosynthetic process |
| A | 0006657 | biological_process | CDP-choline pathway |
| A | 0008654 | biological_process | phospholipid biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004103 | molecular_function | choline kinase activity |
| B | 0004305 | molecular_function | ethanolamine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006646 | biological_process | phosphatidylethanolamine biosynthetic process |
| B | 0006657 | biological_process | CDP-choline pathway |
| B | 0008654 | biological_process | phospholipid biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX B 1001 |
| Chain | Residue |
| B | GLU245 |
| B | GLU283 |
| B | TYR286 |
| B | TYR288 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX B 1002 |
| Chain | Residue |
| B | TRP187 |
| B | HOH1046 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX B 1003 |
| Chain | Residue |
| B | ASP372 |
| B | TRP293 |
| B | GLY369 |
| B | LEU371 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX A 1004 |
| Chain | Residue |
| A | TRP187 |
| A | HOH1061 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX B 1005 |
| Chain | Residue |
| B | ARG194 |
| B | TYR195 |
| B | GLN198 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX B 1006 |
| Chain | Residue |
| B | GLY77 |
| B | LEU78 |
| B | GLN244 |
| B | HOH1156 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX A 1007 |
| Chain | Residue |
| A | SER79 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX B 1008 |
| Chain | Residue |
| B | GLU178 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX A 1009 |
| Chain | Residue |
| A | GLN198 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX B 1010 |
| Chain | Residue |
| B | GLU46 |
| B | PRO66 |
| B | LEU69 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UNX A 1011 |
| Chain | Residue |
| A | ARG54 |
| A | GLU55 |
| A | LEU57 |
| A | ARG62 |
| B | LYS183 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX A 1012 |
| Chain | Residue |
| A | SER217 |
| A | LYS219 |
| A | ASP220 |
| site_id | BC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE UNX A 1013 |
| Chain | Residue |
| A | ARG314 |
| site_id | BC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX B 1014 |
| Chain | Residue |
| B | TRP52 |
| B | GLU55 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UNX B 1015 |
| Chain | Residue |
| A | LYS183 |
| B | ARG54 |
| B | GLU55 |
| B | LEU57 |
| B | ARG62 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX A 1016 |
| Chain | Residue |
| A | ARG70 |
| A | TYR72 |
| A | ARG84 |
| A | SER86 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX B 1017 |
| Chain | Residue |
| B | TYR72 |
| B | CYS85 |
| B | SER86 |
| B | GLU100 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX B 1018 |
| Chain | Residue |
| B | VAL113 |
| B | ASP114 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UNX B 1019 |
| Chain | Residue |
| B | LYS170 |
| B | ASP258 |
| B | SER259 |
| B | LEU260 |
| B | HOH1045 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX B 1020 |
| Chain | Residue |
| B | HIS311 |
| B | ARG314 |
| B | HIS315 |
| site_id | CC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE UNX B 1021 |
| Chain | Residue |
| B | LEU102 |
| B | ILE148 |
| site_id | CC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE UNX B 1022 |
| Chain | Residue |
| B | GLY132 |
| B | GLN134 |
| B | GLN146 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE UNX B 1023 |
| Chain | Residue |
| B | ASN80 |
| B | ARG104 |
| B | ASP264 |
| B | GLU266 |
| B | HOH1110 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE UNX A 1024 |
| Chain | Residue |
| A | GLU245 |
| A | GLU283 |
| A | TYR286 |
| A | TYR288 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P35790","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"20299452","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human choline kinase beta in complex with phosphorylated hemicholinium-3 and adenosine nucleotide.","authoringGroup":["Structural genomics consortium (SGC)"]}},{"source":"PDB","id":"3FEG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
