4MVD
Crystal Structure of a Mammalian Cytidylyltransferase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004105 | molecular_function | choline-phosphate cytidylyltransferase activity |
| A | 0006657 | biological_process | CDP-choline pathway |
| A | 0009058 | biological_process | biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004105 | molecular_function | choline-phosphate cytidylyltransferase activity |
| B | 0006657 | biological_process | CDP-choline pathway |
| B | 0009058 | biological_process | biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004105 | molecular_function | choline-phosphate cytidylyltransferase activity |
| C | 0006657 | biological_process | CDP-choline pathway |
| C | 0009058 | biological_process | biosynthetic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004105 | molecular_function | choline-phosphate cytidylyltransferase activity |
| D | 0006657 | biological_process | CDP-choline pathway |
| D | 0009058 | biological_process | biosynthetic process |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0004105 | molecular_function | choline-phosphate cytidylyltransferase activity |
| E | 0006657 | biological_process | CDP-choline pathway |
| E | 0009058 | biological_process | biosynthetic process |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0004105 | molecular_function | choline-phosphate cytidylyltransferase activity |
| F | 0006657 | biological_process | CDP-choline pathway |
| F | 0009058 | biological_process | biosynthetic process |
| G | 0003824 | molecular_function | catalytic activity |
| G | 0004105 | molecular_function | choline-phosphate cytidylyltransferase activity |
| G | 0006657 | biological_process | CDP-choline pathway |
| G | 0009058 | biological_process | biosynthetic process |
| H | 0003824 | molecular_function | catalytic activity |
| H | 0004105 | molecular_function | choline-phosphate cytidylyltransferase activity |
| H | 0006657 | biological_process | CDP-choline pathway |
| H | 0009058 | biological_process | biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CDC B 401 |
| Chain | Residue |
| B | ASP82 |
| B | ARG196 |
| B | THR197 |
| B | ILE200 |
| B | GLY83 |
| B | ILE84 |
| B | PHE85 |
| B | ALA95 |
| B | PRO150 |
| B | TRP151 |
| B | ASP169 |
| B | GLN195 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CDC A 401 |
| Chain | Residue |
| A | ASP82 |
| A | GLY83 |
| A | ILE84 |
| A | PHE85 |
| A | GLY91 |
| A | ALA95 |
| A | TRP151 |
| A | ASP169 |
| A | GLN195 |
| A | ARG196 |
| A | THR197 |
| A | ILE200 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CDC D 401 |
| Chain | Residue |
| D | ASP82 |
| D | GLY83 |
| D | ILE84 |
| D | PHE85 |
| D | ALA95 |
| D | PRO150 |
| D | TRP151 |
| D | ASP169 |
| D | GLN195 |
| D | ARG196 |
| D | THR197 |
| D | ILE200 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CDC C 401 |
| Chain | Residue |
| C | ASP82 |
| C | GLY83 |
| C | ILE84 |
| C | PHE85 |
| C | GLY91 |
| C | ALA95 |
| C | TRP151 |
| C | ASP169 |
| C | GLN195 |
| C | ARG196 |
| C | THR197 |
| C | ILE200 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CDC F 401 |
| Chain | Residue |
| F | ASP82 |
| F | GLY83 |
| F | ILE84 |
| F | PHE85 |
| F | ALA95 |
| F | PRO150 |
| F | TRP151 |
| F | ASP169 |
| F | GLN195 |
| F | ARG196 |
| F | THR197 |
| F | ILE200 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CDC E 401 |
| Chain | Residue |
| E | ASP82 |
| E | GLY83 |
| E | ILE84 |
| E | PHE85 |
| E | GLY91 |
| E | ALA95 |
| E | TRP151 |
| E | ASP169 |
| E | GLN195 |
| E | ARG196 |
| E | THR197 |
| E | ILE200 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CDC H 401 |
| Chain | Residue |
| H | ASP82 |
| H | GLY83 |
| H | ILE84 |
| H | PHE85 |
| H | ALA95 |
| H | PRO150 |
| H | TRP151 |
| H | ASP169 |
| H | GLN195 |
| H | ARG196 |
| H | THR197 |
| H | ILE200 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE CDC G 401 |
| Chain | Residue |
| G | ASP82 |
| G | GLY83 |
| G | ILE84 |
| G | PHE85 |
| G | GLY91 |
| G | ALA95 |
| G | TRP151 |
| G | ASP169 |
| G | GLN195 |
| G | ARG196 |
| G | THR197 |
| G | ILE200 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 48 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:19783652, ECO:0000305|PubMed:24275660, ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC, ECO:0007744|PDB:4MVD |
| Chain | Residue | Details |
| B | ILE84 | |
| A | ARG196 | |
| A | THR197 | |
| A | ILE200 | |
| D | ILE84 | |
| D | PHE85 | |
| D | GLN195 | |
| D | ARG196 | |
| D | THR197 | |
| D | ILE200 | |
| C | ILE84 | |
| B | PHE85 | |
| C | PHE85 | |
| C | GLN195 | |
| C | ARG196 | |
| C | THR197 | |
| C | ILE200 | |
| F | ILE84 | |
| F | PHE85 | |
| F | GLN195 | |
| F | ARG196 | |
| F | THR197 | |
| B | GLN195 | |
| F | ILE200 | |
| E | ILE84 | |
| E | PHE85 | |
| E | GLN195 | |
| E | ARG196 | |
| E | THR197 | |
| E | ILE200 | |
| H | ILE84 | |
| H | PHE85 | |
| H | GLN195 | |
| B | ARG196 | |
| H | ARG196 | |
| H | THR197 | |
| H | ILE200 | |
| G | ILE84 | |
| G | PHE85 | |
| G | GLN195 | |
| G | ARG196 | |
| G | THR197 | |
| G | ILE200 | |
| B | THR197 | |
| B | ILE200 | |
| A | ILE84 | |
| A | PHE85 | |
| A | GLN195 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19783652, ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC, ECO:0007744|PDB:4MVD |
| Chain | Residue | Details |
| B | HIS92 | |
| A | HIS92 | |
| D | HIS92 | |
| C | HIS92 | |
| F | HIS92 | |
| E | HIS92 | |
| H | HIS92 | |
| G | HIS92 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:19783652, ECO:0000305|PubMed:24275660, ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC |
| Chain | Residue | Details |
| B | LYS122 | |
| D | HIS168 | |
| D | ASP169 | |
| D | TYR173 | |
| C | LYS122 | |
| C | HIS168 | |
| C | ASP169 | |
| C | TYR173 | |
| F | LYS122 | |
| F | HIS168 | |
| F | ASP169 | |
| B | HIS168 | |
| F | TYR173 | |
| E | LYS122 | |
| E | HIS168 | |
| E | ASP169 | |
| E | TYR173 | |
| H | LYS122 | |
| H | HIS168 | |
| H | ASP169 | |
| H | TYR173 | |
| G | LYS122 | |
| B | ASP169 | |
| G | HIS168 | |
| G | ASP169 | |
| G | TYR173 | |
| B | TYR173 | |
| A | LYS122 | |
| A | HIS168 | |
| A | ASP169 | |
| A | TYR173 | |
| D | LYS122 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:19783652, ECO:0000305|PubMed:24275660, ECO:0007744|PDB:3HL4 |
| Chain | Residue | Details |
| B | TRP151 | |
| A | TRP151 | |
| D | TRP151 | |
| C | TRP151 | |
| F | TRP151 | |
| E | TRP151 | |
| H | TRP151 | |
| G | TRP151 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P49585 |
| Chain | Residue | Details |
| B | MET1 | |
| A | MET1 | |
| D | MET1 | |
| C | MET1 | |
| F | MET1 | |
| E | MET1 | |
| H | MET1 | |
| G | MET1 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P49585 |
| Chain | Residue | Details |
| B | LYS8 | |
| A | LYS8 | |
| D | LYS8 | |
| C | LYS8 | |
| F | LYS8 | |
| E | LYS8 | |
| H | LYS8 | |
| G | LYS8 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49585 |
| Chain | Residue | Details |
| B | SER233 | |
| A | SER233 | |
| D | SER233 | |
| C | SER233 | |
| F | SER233 | |
| E | SER233 | |
| H | SER233 | |
| G | SER233 |
