8BR9
Stapled peptide SP24 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 | DNA repair and recombination protein RadA | polymer | 231 | 25542.1 | 1 | UniProt (O74036) Pfam (PF08423) In PDB | Pyrococcus furiosus | Humanised RadA mutant HumRadA22 |
2 | B | Breast cancer type 2 susceptibility protein | polymer | 38 | 3985.5 | 1 | UniProt (P51587) Pfam (PF00634) In PDB | Homo sapiens (human) | Fanconi anemia group D1 protein |
3 | A | ADENOSINE-5'-DIPHOSPHATE | non-polymer | 427.2 | 1 | Chemie (ADP) | |||
4 | B | 4,6-diethylpyrimidin-2-amine | non-polymer | 151.2 | 1 | Chemie (RF6) | |||
5 | water | water | 18.0 | 82 | Chemie (HOH) |
Sequence modifications
A: 107 - 349 (UniProt: O74036)
B: 1226 - 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 | engineered mutation |
Gln 1232 | Glu 1232 | engineered mutation |
Cys 1238 | Val 1238 | engineered mutation |
Val 2050 | Glu 1249 | engineered mutation |
Asn 2051 | Glu 1250 | engineered mutation |
Ser 2052 | Thr 1251 | engineered mutation |
Phe 2055 | Glu 1254 | engineered mutation |
Ser 2056 | Val 1255 | engineered mutation |
Gly 2057 | His 1256 | engineered mutation |
Phe 2058 | Pro 1257 | engineered mutation |
Ser 2059 | Ile 1258 | engineered mutation |
Thr 2060 | Ser 1259 | engineered mutation |
Ala 2061 | Leu 1260 | engineered mutation |
Gly 2063 | Ser 1262 | engineered mutation |
Lys 2064 | Ser 1263 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 29527.6 | |
Non-Polymers* | Number of molecules | 2 |
Total formula weight | 578.4 | |
All* | Total formula weight | 30106.0 |