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 | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19783652, ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC, ECO:0007744|PDB:4MVD |
Chain | Residue | Details |
B | ILE84 | |
F | ARG196 | |
E | ILE84 | |
E | ARG196 | |
H | ILE84 | |
H | ARG196 | |
G | ILE84 | |
G | ARG196 | |
B | ARG196 | |
A | ILE84 | |
A | ARG196 | |
D | ILE84 | |
D | ARG196 | |
C | ILE84 | |
C | ARG196 | |
F | ILE84 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19783652, ECO:0007744|PDB:3HL4, ECO:0007744|PDB:4MVC |
Chain | Residue | Details |
B | LYS122 | |
C | LYS122 | |
C | HIS168 | |
C | TYR173 | |
F | LYS122 | |
F | HIS168 | |
F | TYR173 | |
E | LYS122 | |
E | HIS168 | |
E | TYR173 | |
H | LYS122 | |
B | HIS168 | |
H | HIS168 | |
H | TYR173 | |
G | LYS122 | |
G | HIS168 | |
G | TYR173 | |
B | TYR173 | |
A | LYS122 | |
A | HIS168 | |
A | TYR173 | |
D | LYS122 | |
D | HIS168 | |
D | TYR173 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19783652, 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_FI4 |
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_FI5 |
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_FI6 |
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 |