eF-site ID 2mej_8-AB PDB Code 2mej Model 8 Chain A, B click to enlarge Title Solution Structure of the Complex Between BCL-xL and the p53 Core Domain determined with PRE restraints Classification APOPTOSIS Compound Bcl-2-like protein 1 Source null (P53_HUMAN) Sequence A:  MSQSNRELVVDFLSYKLSQKGYSWSQFSMAAVKQALREAG DEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDG VNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYL NDHLEPWIQENGGWDTFVELYGNN B:  SVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFC QLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRR CPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHS VVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTII TLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLR Description Functional site 1) chain B residue 176 type sequence C description BINDING SITE FOR RESIDUE ZN B 401 source : AC1 2) chain B residue 179 type sequence H description BINDING SITE FOR RESIDUE ZN B 401 source : AC1 3) chain B residue 238 type sequence C description BINDING SITE FOR RESIDUE ZN B 401 source : AC1 4) chain B residue 242 type sequence C description BINDING SITE FOR RESIDUE ZN B 401 source : AC1 5) chain B residue 120 type MOD_RES sequence K description N6-acetyllysine; by KAT6A => ECO:0000269|PubMed:23431171 source Swiss-Prot : SWS_FT_FI4 6) chain B residue 183 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI5 7) chain B residue 269 type MOD_RES sequence S description Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI5 8) chain B residue 284 type MOD_RES sequence T description Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462 source Swiss-Prot : SWS_FT_FI6 9) 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 10) chain B residue 237-249 type prosite sequence MCNSSCMGGMNRR description P53 p53 family signature. MCNSSCMGGMNRR source prosite : PS00348 11) chain A residue 133-151 type prosite sequence LFRDGVNWGRIVAFFSFGG description BH1 Apoptosis regulator, Bcl-2 family BH1 motif signature. LFrDGv.NWGRIVAFFsFGG source prosite : PS01080 12) chain A residue 184-195 type prosite sequence WIQENGGWDTFV description BH2 Apoptosis regulator, Bcl-2 family BH2 motif signature. WIqenGGWDtFV source prosite : PS01258 13) chain A residue 89-103 type prosite sequence VKQALREAGDEFELR description BH3 Apoptosis regulator, Bcl-2 family BH3 motif signature. VkqaLReAGDEFELR source prosite : PS01259 14) chain A residue 7-27 type prosite sequence SNRELVVDFLSYKLSQKGYSW description BH4_1 Apoptosis regulator, Bcl-2 family BH4 motif signature. SNRELVvDFLSYKLSQKGYsW source prosite : PS01260 15) 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 16) 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 17) 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 18) 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

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