eF-site ID 1kzy-ABCD PDB Code 1kzy Chain A, B, C, D click to enlarge Title Crystal Structure of the 53bp1 BRCT Region Complexed to Tumor Suppressor P53 Classification DNA BINDING PROTEIN, PROTEIN BINDING Compound CELLULAR TUMOR ANTIGEN P53 Source null (TP53B_HUMAN) Sequence A:  SSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMF CQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVR RCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRH SVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTI ITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENL B:  SSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMF CQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVR RCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRH SVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTI ITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENL C:  ALEEQRGPLPLNKTLFLGYAFLLTMATIPPFNKQYTESQL RAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLA SGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRIL DWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASV KQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLP VVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH D:  ALEEQRGPLPLNKTLFLGYAFLLTMATIPPFNKQYTESQL RAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLA SGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRIL DWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASV KQHHSSAHNKDIALGVFDVVVTDPSCPASVLKCAEALQLP VVSQEWVIQCLIVGERIGFKQHPKYKHDYVSH Description (1)  CELLULAR TUMOR ANTIGEN P53, TUMOR REPRESSOR P53-BINDING PROTEIN 1 Functional site 1) chain A residue 176 type sequence C description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 2) chain A residue 179 type sequence H description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 3) chain A residue 238 type sequence C description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 4) chain A residue 242 type sequence C description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 5) chain B residue 176 type sequence C description BINDING SITE FOR RESIDUE ZN B 1 source : AC2 6) chain B residue 179 type sequence H description BINDING SITE FOR RESIDUE ZN B 1 source : AC2 7) chain B residue 238 type sequence C description BINDING SITE FOR RESIDUE ZN B 1 source : AC2 8) chain B residue 242 type sequence C description BINDING SITE FOR RESIDUE ZN B 1 source : AC2 9) chain C residue 1778 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:21144835 source Swiss-Prot : SWS_FT_FI2 10) chain D residue 1778 type MOD_RES sequence S description Phosphoserine => ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:21144835 source Swiss-Prot : SWS_FT_FI2 11) chain A residue 120 type MOD_RES sequence K description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171 source Swiss-Prot : SWS_FT_FI3 12) chain B residue 120 type MOD_RES sequence K description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171 source Swiss-Prot : SWS_FT_FI3 13) chain A residue 183 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI4 14) chain A residue 269 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI4 15) chain B residue 183 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI4 16) chain B residue 269 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI4 17) chain A residue 284 type MOD_RES sequence T description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI5 18) chain B residue 284 type MOD_RES sequence T description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI5 19) chain B residue 176 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI1 20) chain B residue 179 type MOD_RES sequence H description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI1 21) chain B residue 238 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 242 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI1 23) chain A residue 238 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI1 24) chain A residue 242 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18669648 source Swiss-Prot : SWS_FT_FI1 25) chain A residue 237-249 type prosite sequence MCNSSCMGGMNRR description P53 p53 family signature. MCNSSCMGGMNRR source prosite : PS00348

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