eF-site ID 5ecg-ABCD PDB Code 5ecg Chain A, B, C, D click to enlarge Title Crystal structure of the BRCT domains of 53BP1 in complex with p53 and H2AX-pSer139 (gammaH2AX) Classification ANTITUMOR PROTEIN Compound Cellular tumor antigen p53 Source Homo sapiens (Human) (5ECG) Sequence A:  SVPSQKTYQGSYGFRLGFLHSSVTCTYSPALNKMFCQLAK TCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHH ERCSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYE PPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSS GNLLGRNSFEVRVCACPGRDRRTEEENLRKKG B:  SVPSQKTYQGSYGFRLGFLVTCTYSPALNKMFCQLAKTCP VQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERC GLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVG SDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLG RNSFEVRVCACPGRDRRTEEENL C:  ALEEQRGPLPLNKTLFLGYAFLLTMATTIPPFNKQYTESQ LRAGAGYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCL ASGIPCVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRI LDWQPRENPFQNLKVLLVSDQQQNFLELWSEILMTGGAAS VKQHHSSAIALGVFDVVVTDPSCPASVLKCAEALQLPVVS QEWVIQCLIVGERIGFKQHPKYKHDYV D:  RGPLPLNKTLFLGYAFLLTMATEIPPFNKQYTESQLRAGA GYILEDFNEAQCNTAYQCLLIADQHCRTRKYFLCLASGIP CVSHVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQP RENPFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHH SSADIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWV IQCLIVGERIGFKQHPKYKHDYV 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 B residue 176 type sequence C description binding site for residue ZN B 401 source : AC2 6) chain B residue 179 type sequence H description binding site for residue ZN B 401 source : AC2 7) chain B residue 238 type sequence C description binding site for residue ZN B 401 source : AC2 8) chain B residue 242 type sequence C description binding site for residue ZN B 401 source : AC2 9) chain D residue 1737 type sequence T description binding site for Di-peptide SEP E 139 and GLN E 140 source : AC3 10) chain D residue 1738 type sequence M description binding site for Di-peptide SEP E 139 and GLN E 140 source : AC3 11) chain D residue 1740 type sequence T description binding site for Di-peptide SEP E 139 and GLN E 140 source : AC3 12) chain D residue 1773 type sequence K description binding site for Di-peptide SEP E 139 and GLN E 140 source : AC3 13) chain D residue 1812 type sequence T description binding site for Di-peptide SEP E 139 and GLN E 140 source : AC3 14) chain D residue 1814 type sequence K description binding site for Di-peptide SEP E 139 and GLN E 140 source : AC3 15) chain C residue 1737 type sequence T description binding site for Di-peptide SEP F 139 and GLN F 140 source : AC4 16) chain C residue 1738 type sequence M description binding site for Di-peptide SEP F 139 and GLN F 140 source : AC4 17) chain C residue 1740 type sequence T description binding site for Di-peptide SEP F 139 and GLN F 140 source : AC4 18) chain C residue 1773 type sequence K description binding site for Di-peptide SEP F 139 and GLN F 140 source : AC4 19) chain C residue 1812 type sequence T description binding site for Di-peptide SEP F 139 and GLN F 140 source : AC4 20) chain C residue 1814 type sequence K description binding site for Di-peptide SEP F 139 and GLN F 140 source : AC4 21) chain D residue 1797 type sequence N description binding site for Di-peptide SEP F 139 and GLN F 140 source : AC4 22) chain D residue 1798 type sequence T description binding site for Di-peptide SEP F 139 and GLN F 140 source : AC4 23) 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 24) 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 25) chain A residue 238 type MOD_RES sequence C description Phosphoserine => ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:21144835 source Swiss-Prot : SWS_FT_FI2 26) chain A residue 242 type MOD_RES sequence C description Phosphoserine => ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:21144835 source Swiss-Prot : SWS_FT_FI2 27) chain B residue 176 type MOD_RES sequence C description Phosphoserine => ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:21144835 source Swiss-Prot : SWS_FT_FI2 28) chain B residue 179 type MOD_RES sequence H description Phosphoserine => ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:21144835 source Swiss-Prot : SWS_FT_FI2 29) chain B residue 238 type MOD_RES sequence C description Phosphoserine => ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:21144835 source Swiss-Prot : SWS_FT_FI2 30) chain B residue 242 type MOD_RES sequence C description Phosphoserine => ECO:0000269|PubMed:19176521, ECO:0000269|PubMed:21144835 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 269 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI5 32) chain B residue 269 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 284 type MOD_RES sequence T description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI6 34) chain B residue 284 type MOD_RES sequence T description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI6 35) 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 36) 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 37) chain A residue 237-249 type prosite sequence MCNSSCMGGMNRR description P53 p53 family signature. MCNSSCMGGMNRR source prosite : PS00348

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