4MSK
Co-crystal structure of tankyrase 1 with compound 34
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003950 | molecular_function | NAD+-protein poly-ADP-ribosyltransferase activity |
| B | 0003950 | molecular_function | NAD+-protein poly-ADP-ribosyltransferase activity |
| C | 0003950 | molecular_function | NAD+-protein poly-ADP-ribosyltransferase activity |
| D | 0003950 | molecular_function | NAD+-protein poly-ADP-ribosyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 1401 |
| Chain | Residue |
| A | CYS1234 |
| A | HIS1237 |
| A | CYS1242 |
| A | CYS1245 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 2C8 A 1402 |
| Chain | Residue |
| A | LYS1195 |
| A | GLY1196 |
| A | PHE1197 |
| A | ASP1198 |
| A | HIS1201 |
| A | TYR1203 |
| A | ILE1212 |
| A | TYR1213 |
| A | PHE1214 |
| A | ALA1215 |
| A | LYS1220 |
| A | SER1221 |
| A | TYR1224 |
| A | GLU1291 |
| A | HOH1526 |
| A | HIS1184 |
| A | GLY1185 |
| A | SER1186 |
| A | PHE1188 |
| A | ALA1191 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 1401 |
| Chain | Residue |
| B | CYS1234 |
| B | HIS1237 |
| B | CYS1242 |
| B | CYS1245 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 2C8 B 1402 |
| Chain | Residue |
| B | HIS1184 |
| B | GLY1185 |
| B | PHE1188 |
| B | ALA1191 |
| B | GLY1196 |
| B | PHE1197 |
| B | ASP1198 |
| B | HIS1201 |
| B | TYR1203 |
| B | ILE1212 |
| B | TYR1213 |
| B | PHE1214 |
| B | ALA1215 |
| B | LYS1220 |
| B | SER1221 |
| B | TYR1224 |
| B | GLU1291 |
| B | HOH1516 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN C 1401 |
| Chain | Residue |
| C | HIS1237 |
| C | CYS1242 |
| C | CYS1245 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 2C8 C 1402 |
| Chain | Residue |
| C | HIS1184 |
| C | GLY1185 |
| C | PHE1188 |
| C | LYS1195 |
| C | GLY1196 |
| C | PHE1197 |
| C | ASP1198 |
| C | HIS1201 |
| C | TYR1203 |
| C | ILE1212 |
| C | TYR1213 |
| C | PHE1214 |
| C | ALA1215 |
| C | LYS1220 |
| C | SER1221 |
| C | TYR1224 |
| C | GLU1291 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN D 1401 |
| Chain | Residue |
| D | CYS1234 |
| D | HIS1237 |
| D | CYS1242 |
| D | CYS1245 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 2C8 D 1402 |
| Chain | Residue |
| D | HIS1184 |
| D | GLY1185 |
| D | SER1186 |
| D | PHE1188 |
| D | ALA1191 |
| D | LYS1195 |
| D | GLY1196 |
| D | PHE1197 |
| D | ASP1198 |
| D | HIS1201 |
| D | TYR1203 |
| D | TYR1213 |
| D | PHE1214 |
| D | ALA1215 |
| D | LYS1220 |
| D | SER1221 |
| D | TYR1224 |
| D | GLU1291 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18436240, ECO:0007744|PDB:2RF5, ECO:0007744|PDB:3UDD, ECO:0007744|PDB:3UH2, ECO:0007744|PDB:3UH4, ECO:0007744|PDB:4DVI, ECO:0007744|PDB:4I9I, ECO:0007744|PDB:4K4E, ECO:0007744|PDB:4K4F, ECO:0007744|PDB:4KRS, ECO:0007744|PDB:4LI6, ECO:0007744|PDB:4LI8, ECO:0007744|PDB:4MSG, ECO:0007744|PDB:4MSK, ECO:0007744|PDB:4MT9, ECO:0007744|PDB:4N3R, ECO:0007744|PDB:4N4V, ECO:0007744|PDB:4OA7, ECO:0007744|PDB:4TOR, ECO:0007744|PDB:4TOS, ECO:0007744|PDB:4W5S, ECO:0007744|PDB:4W6E |
| Chain | Residue | Details |
| A | CYS1234 | |
| C | HIS1237 | |
| C | CYS1242 | |
| C | CYS1245 | |
| D | CYS1234 | |
| D | HIS1237 | |
| D | CYS1242 | |
| D | CYS1245 | |
| A | HIS1237 | |
| A | CYS1242 | |
| A | CYS1245 | |
| B | CYS1234 | |
| B | HIS1237 | |
| B | CYS1242 | |
| B | CYS1245 | |
| C | CYS1234 |
