8C3J
Stapled peptide SP2 in complex with humanised RadA mutant HumRadA22
Entity
Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
1 | A, B | DNA repair and recombination protein RadA | polymer | 231 | 25542.1 | 2 | UniProt (O74036) Pfam (PF08423) UniProt (by SIFTS) (Q06609) In PDB | Pyrococcus furiosus | Humanised RadA mutant HumRadA22 |
2 | C, J | Breast cancer type 2 susceptibility protein | polymer | 36 | 3687.2 | 2 | UniProt (P51587) Pfam (PF00634) In PDB | Homo sapiens (human) | Fanconi anemia group D1 protein |
3 | C | 2-[(4,6-diethyl-1,3,5-triazin-2-yl)-methyl-amino]ethanoic acid | non-polymer | 224.3 | 1 | Chemie (TKI) |
Sequence modifications
A, B: 107 - 349 (UniProt: O74036)
C, J: 1226 - 1244 (UniProt: P51587)
C, J: 2050 - 2064 (UniProt: P51587)
PDB | External Database | Details |
---|---|---|
Met 107 | Arg 107 | engineered mutation |
Ala 168 | Val 168 | engineered mutation |
Met 169 | Ile 169 | engineered mutation |
Tyr 170 | Trp 170 | engineered mutation |
Leu 182 | Ile 182 | engineered mutation |
Asp 198 | Lys 198 | engineered mutation |
Asn 199 | His 199 | engineered mutation |
Val 200 | Ile 200 | engineered mutation |
Ala 201 | Tyr 201 | engineered mutation |
Tyr 202 | Val 202 | engineered mutation |
Gln 213 | Leu 213 | engineered mutation |
Leu 215 | Val 215 | engineered mutation |
Tyr 216 | Gln 216 | engineered mutation |
Ser 219 | Glu 219 | engineered mutation |
Ala 220 | Asp 220 | engineered mutation |
Met 221 | Lys 221 | engineered mutation |
Met 222 | Ile 222 | engineered mutation |
Val 223 | Lys 223 | engineered mutation |
Ser 225 | Leu 225 | engineered mutation |
Tyr 232 | Val 232 | engineered mutation |
Arg 263 | Lys 263 | engineered mutation |
Phe 264 | His 264 | engineered mutation |
Arg 266 | Ala 266 | engineered mutation |
Met 267 | Asp 267 | engineered mutation |
Glu 274 | Leu 274 | engineered mutation |
Phe 275 | Tyr 275 | engineered mutation |
Asn 300 | Arg 288 | engineered mutation |
- | Pro 289 | deletion |
- | Asp 290 | deletion |
- | Ala 291 | deletion |
- | Phe 292 | deletion |
- | Phe 293 | deletion |
- | Gly 294 | deletion |
- | Asp 295 | deletion |
- | Pro 296 | deletion |
- | Thr 297 | deletion |
- | Arg 298 | deletion |
- | Pro 299 | deletion |
- | Ile 300 | deletion |
PDB | External Database | Details |
---|---|---|
Cys 1231 | Thr 1231 | conflict |
Cys 1238 | Val 1238 | conflict |
PDB | External Database | Details |
---|---|---|
Gly 2048 | - | linker |
Ser 2049 | - | linker |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 4 |
Total formula weight | 58458.5 | |
Non-Polymers* | Number of molecules | 1 |
Total formula weight | 224.3 | |
All* | Total formula weight | 58682.7 |