eF-site ID 1gzh-ABCD PDB Code 1gzh Chain A, B, C, D click to enlarge Title Crystal structure of the BRCT domains of human 53BP1 bound to the p53 tumor supressor Classification GENE REGULATION Compound CELLULAR TUMOR ANTIGEN P53 Source Homo sapiens (Human) (P53_HUMAN) Sequence A:  SSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMF CQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVR RCPHHERCAPPQHLIRVEGLRVEYLDDRNTFRHSVVVPYE PPECTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLL GRNSFEVRVCACPGRDRRTEEENLRKK B:  LNKTLFLGYAFLLTMATTSDKLASRSPPFNKQYTESQLRA GAGYILEDFNTAYQCLLIADQHCRTRKYFLCLASGIPCVS HVWVHDSCHANQLQNYRNYLLPAGYSLEEQRILDWQPREN PFQNLKVLLVSDQQQNFLELWSEILMTGGAASVKQHHSSA HNKDIALGVFDVVVTDPSCPASVLKCAEALQLPVVSQEWV IQCLIVGERIGFKQHPKYKHDYVSH C:  SSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMF CQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVR RCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRH SVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTI ITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLR D:  NKTLFLGYAFLLTMATFNKQYTESQLRAGAGYILEDFNEN TAYQCLLIADQHCRTRKYFLCLASGIPCVSHVWVHDSCHA NQLQNYRNYLLPAGYSLEEQRILDWQPRENPFQNLKVLLV SDQQQNFLELWSEILMTGGAASVKQHHSSAHNKDIALGVF DVVVTDPSCPASVLKCAEALQLPVVSQEWVIQCLIVGERI GFKQHPKYKHDYV Description Functional site 1) chain A residue 176 type sequence C description BINDING SITE FOR RESIDUE ZN A 1293 source : AC1 2) chain A residue 179 type sequence H description BINDING SITE FOR RESIDUE ZN A 1293 source : AC1 3) chain A residue 238 type sequence C description BINDING SITE FOR RESIDUE ZN A 1293 source : AC1 4) chain A residue 242 type sequence C description BINDING SITE FOR RESIDUE ZN A 1293 source : AC1 5) chain B residue 1737 type sequence T description BINDING SITE FOR RESIDUE SO4 B 2972 source : AC2 6) chain B residue 1738 type sequence M description BINDING SITE FOR RESIDUE SO4 B 2972 source : AC2 7) chain B residue 1773 type sequence K description BINDING SITE FOR RESIDUE SO4 B 2972 source : AC2 8) chain B residue 1814 type sequence K description BINDING SITE FOR RESIDUE SO4 B 2972 source : AC2 9) chain C residue 183 type sequence S description BINDING SITE FOR RESIDUE SO4 B 2972 source : AC2 10) chain C residue 176 type sequence C description BINDING SITE FOR RESIDUE ZN C 1290 source : AC3 11) chain C residue 179 type sequence H description BINDING SITE FOR RESIDUE ZN C 1290 source : AC3 12) chain C residue 238 type sequence C description BINDING SITE FOR RESIDUE ZN C 1290 source : AC3 13) chain C residue 242 type sequence C description BINDING SITE FOR RESIDUE ZN C 1290 source : AC3 14) chain B residue 1798 type sequence T description BINDING SITE FOR RESIDUE SO4 D 2970 source : AC4 15) chain D residue 1736 type sequence L description BINDING SITE FOR RESIDUE SO4 D 2970 source : AC4 16) chain D residue 1737 type sequence T description BINDING SITE FOR RESIDUE SO4 D 2970 source : AC4 17) chain D residue 1738 type sequence M description BINDING SITE FOR RESIDUE SO4 D 2970 source : AC4 18) chain D residue 1773 type sequence K description BINDING SITE FOR RESIDUE SO4 D 2970 source : AC4 19) chain D residue 1814 type sequence K description BINDING SITE FOR RESIDUE SO4 D 2970 source : AC4 20) chain C 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 21) chain C 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 22) chain C 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 23) chain C 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 24) chain C residue 120 type MOD_RES sequence K description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171 source Swiss-Prot : SWS_FT_FI4 25) chain C residue 183 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI5 26) chain C residue 269 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI5 27) chain C residue 284 type MOD_RES sequence T description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI6 28) chain C 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 29) chain A residue 237-249 type prosite sequence MCNSSCMGGMNRR description P53 p53 family signature. MCNSSCMGGMNRR source prosite : PS00348 30) chain C residue 237-249 type prosite sequence MCNSSCMGGMNRR description P53 p53 family signature. MCNSSCMGGMNRR source prosite : PS00348

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