4MVC
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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE CDC A 401 |
Chain | Residue |
A | ASP82 |
A | HIS168 |
A | ASP169 |
A | TYR173 |
A | TYR182 |
A | GLN195 |
A | ARG196 |
A | THR197 |
A | ILE200 |
A | HOH504 |
A | GLY83 |
A | ILE84 |
A | PHE85 |
A | HIS89 |
A | GLY91 |
A | ALA95 |
A | LYS122 |
A | TRP151 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE CDC B 401 |
Chain | Residue |
B | ASP82 |
B | GLY83 |
B | ILE84 |
B | PHE85 |
B | HIS89 |
B | GLY91 |
B | HIS92 |
B | ALA95 |
B | LYS122 |
B | PRO150 |
B | TRP151 |
B | HIS168 |
B | ASP169 |
B | TYR173 |
B | TYR182 |
B | GLN195 |
B | ARG196 |
B | THR197 |
B | ILE200 |
B | HOH502 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
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 |
A | ILE84 | |
B | ARG196 | |
B | THR197 | |
B | ILE200 | |
A | PHE85 | |
A | GLN195 | |
A | ARG196 | |
A | THR197 | |
A | ILE200 | |
B | ILE84 | |
B | PHE85 | |
B | GLN195 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19783652, ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC, ECO:0007744|PDB:4MVD |
Chain | Residue | Details |
A | HIS92 | |
B | HIS92 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000305|PubMed:19783652, ECO:0000305|PubMed:24275660, ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC |
Chain | Residue | Details |
A | LYS122 | |
A | HIS168 | |
A | ASP169 | |
A | TYR173 | |
B | LYS122 | |
B | HIS168 | |
B | ASP169 | |
B | TYR173 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000305|PubMed:19783652, ECO:0000305|PubMed:24275660, ECO:0007744|PDB:3HL4 |
Chain | Residue | Details |
A | TRP151 | |
B | TRP151 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P49585 |
Chain | Residue | Details |
A | MET1 | |
B | MET1 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P49585 |
Chain | Residue | Details |
A | LYS8 | |
B | LYS8 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P49585 |
Chain | Residue | Details |
A | SER265 | |
B | SER265 |