eF-site ID 6ggb-B PDB Code 6ggb Chain B click to enlarge Title p53 cancer mutant Y220C in complex with small-molecule stabilizer PK9318 Classification DNA BINDING PROTEIN Compound Cellular tumor antigen p53 Source (P53_HUMAN) Sequence B:  SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKL FCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVV RRCPHHERCSDSDGLAPPQHLIRVEGNLRAEYLDDRNTFR HSVVVPCEPPEVGSDCTTIHYNYMCYSSCMGGMNRRPILT IITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENLRK Description Functional site 1) chain B residue 176 type sequence C description binding site for residue ZN B 401 source : AC4 2) chain B residue 179 type sequence H description binding site for residue ZN B 401 source : AC4 3) chain B residue 238 type sequence C description binding site for residue ZN B 401 source : AC4 4) chain B residue 242 type sequence C description binding site for residue ZN B 401 source : AC4 5) chain B residue 174 type sequence R description binding site for residue GOL B 402 source : AC5 6) chain B residue 192 type sequence Q description binding site for residue GOL B 402 source : AC5 7) chain B residue 207 type sequence D description binding site for residue GOL B 402 source : AC5 8) chain B residue 212 type sequence F description binding site for residue GOL B 402 source : AC5 9) chain B residue 214 type sequence H description binding site for residue GOL B 402 source : AC5 10) chain B residue 138 type sequence A description binding site for residue EPE B 403 source : AC6 11) chain B residue 139 type sequence K description binding site for residue EPE B 403 source : AC6 12) chain B residue 140 type sequence T description binding site for residue EPE B 403 source : AC6 13) chain B residue 198 type sequence E description binding site for residue EPE B 403 source : AC6 14) chain B residue 235 type sequence N description binding site for residue EPE B 403 source : AC6 15) chain B residue 145 type sequence L description binding site for residue EXQ B 404 source : AC7 16) chain B residue 147 type sequence V description binding site for residue EXQ B 404 source : AC7 17) chain B residue 151 type sequence P description binding site for residue EXQ B 404 source : AC7 18) chain B residue 220 type sequence C description binding site for residue EXQ B 404 source : AC7 19) chain B residue 221 type sequence E description binding site for residue EXQ B 404 source : AC7 20) chain B residue 222 type sequence P description binding site for residue EXQ B 404 source : AC7 21) chain B residue 223 type sequence P description binding site for residue EXQ B 404 source : AC7 22) chain B residue 228 type sequence D description binding site for residue EXQ B 404 source : AC7 23) chain B residue 230 type sequence T description binding site for residue EXQ B 404 source : AC7 24) chain B residue 284 type MOD_RES sequence T description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI6 25) chain B residue 291 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19536131 source Swiss-Prot : SWS_FT_FI8 26) chain B residue 120 type SITE sequence K description Interaction with DNA => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130 source Swiss-Prot : SWS_FT_FI3 27) chain B residue 120 type MOD_RES sequence K description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171 source Swiss-Prot : SWS_FT_FI4 28) chain B residue 183 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI5 29) chain B residue 269 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI5 30) chain B residue 176 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130 source Swiss-Prot : SWS_FT_FI2 31) chain B residue 179 type BINDING sequence H description BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130 source Swiss-Prot : SWS_FT_FI2 32) chain B residue 238 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130 source Swiss-Prot : SWS_FT_FI2 33) chain B residue 242 type BINDING sequence C description BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130 source Swiss-Prot : SWS_FT_FI2

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