eF-site ID 6ggb-A PDB Code 6ggb Chain A 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 A:  SSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKLF CQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVR RCPHHERCSDSDGLAPPQHLIRVEGNLRAEYLDDRNTFRH SVVVPCEPPEVGSDCTTIHYNYMCYSSCMGGMNRRPILTI ITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENLRKK Description Functional site 1) chain A residue 176 type sequence C description binding site for residue ZN A 401 source : AC1 2) chain A residue 179 type sequence H description binding site for residue ZN A 401 source : AC1 3) chain A residue 238 type sequence C description binding site for residue ZN A 401 source : AC1 4) chain A residue 242 type sequence C description binding site for residue ZN A 401 source : AC1 5) chain A residue 145 type sequence L description binding site for residue EXQ A 402 source : AC2 6) chain A residue 147 type sequence V description binding site for residue EXQ A 402 source : AC2 7) chain A residue 150 type sequence T description binding site for residue EXQ A 402 source : AC2 8) chain A residue 151 type sequence P description binding site for residue EXQ A 402 source : AC2 9) chain A residue 220 type sequence C description binding site for residue EXQ A 402 source : AC2 10) chain A residue 221 type sequence E description binding site for residue EXQ A 402 source : AC2 11) chain A residue 222 type sequence P description binding site for residue EXQ A 402 source : AC2 12) chain A residue 223 type sequence P description binding site for residue EXQ A 402 source : AC2 13) chain A residue 228 type sequence D description binding site for residue EXQ A 402 source : AC2 14) chain A residue 230 type sequence T description binding site for residue EXQ A 402 source : AC2 15) chain A residue 131 type sequence N description binding site for residue EDO A 403 source : AC3 16) chain A residue 252 type sequence L description binding site for residue EDO A 403 source : AC3 17) chain A residue 269 type sequence S description binding site for residue EDO A 403 source : AC3 18) chain A residue 97 type sequence V description binding site for residue EPE B 403 source : AC6 19) chain A residue 169 type sequence M description binding site for residue EPE B 403 source : AC6 20) chain A residue 102-292 type DNA_BIND sequence TYQGSYGFRLGFLHSGTAKSVTCTYSPALNKLFCQLAKTC PVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHER CSDSDGLAPPQHLIRVEGNLRAEYLDDRNTFRHSVVVPCE PPEVGSDCTTIHYNYMCYSSCMGGMNRRPILTIITLEDSS GNLLGRDSFEVRVCACPGRDRRTEEENLRKK description DNA_BIND => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 120 type MOD_RES sequence K description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171 source Swiss-Prot : SWS_FT_FI4 22) chain A residue 183 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI5 23) chain A residue 269 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI5 24) chain A residue 284 type MOD_RES sequence T description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI6 25) chain A 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 A residue 292 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 27) chain A 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 28) chain A 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 29) chain A 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 30) chain A 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 31) chain A 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

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