eF-site ID 5fxy-ABCDEFGH PDB Code 5fxy Chain A, B, C, D, E, F, G, H click to enlarge Title Structure of the human RBBP4:MTA1(464-546) complex Classification TRANSCRIPTION Compound HISTONE-BINDING PROTEIN RBBP4 Source Homo sapiens (Human) (MTA1_HUMAN) Sequence A:  DAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQW LPDVTRPEGKDFSIHRLVLGTHTSDEQNHLVIASVQLPND GEFGGFGSVSGKIEIEIKINHEGEVNRARYMPQNPCIIAT KTPSSDVLVFDYTKHPSKPDPECNPDLRLRGGYGLSWNPN LSGHLLSASDDHTICLWDISAVPGKVVDAKTIFTGHTAVV EDVSWHLLHESLFGSVADDQKLMIWDTRSNNTSKPSHSVD AHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKL HSFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKI GEEQSPEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVI CSVSEDNIMQVWQMAENIYND B:  RQAFYLHTTKLTRIARRLCREILRPWHAARHPYLPINSAA IKAECTARLPEAVRKPLEAVLRYLETHPR C:  DAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQW LPDVTRPEGKDFSIHRLVLGTHTSDEQNHLVIASVQLPND GEFGGFGSVSGKIEIEIKINHEGEVNRARYMPQNPCIIAT KTPSSDVLVFDYTKHPSKPDPECNPDLRLRGGYGLSWNPN LSGHLLSASDDHTICLWDISAVGKVVDAKTIFTGHTAVVE DVSWHLLHESLFGSVADDQKLMIWDTRSNNTSKPSHSVDA HTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLH SFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKIG EEQSPEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVIC SVSEDNIMQVWQMAENIYND D:  RQAFYLHTTKLTRIARRLCREILRPWHAARHPYLPINSAA IKAECTARLPEAVRKPLEAVLRYLETHPR E:  DAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQW LPDVTRPEGKDFSIHRLVLGTHTSDEQNHLVIASVQLPND GEFGGFGSVSGKIEIEIKINHEGEVNRARYMPQNPCIIAT KTPSSDVLVFDYTKHPSKPDPECNPDLRLRGGYGLSWNPN LSGHLLSASDDHTICLWDISAVGKVVDAKTIFTGHTAVVE DVSWHLLHESLFGSVADDQKLMIWDTRSNNTSKPSHSVDA HTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKLH SFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKIG EEQSPEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVIC SVSEDNIMQVWQMAENIYND F:  QAFYLHTTKLTRIARRLCREILRPWHAARHPYLPINSAAI KAECTARLPEAVRKPLEAVLRYLETHPR G:  DAVEERVINEEYKIWKKNTPFLYDLVMTHALEWPSLTAQW LPDVTRPEGKDFSIHRLVLGTHTSDEQNHLVIASVQLPND GEFGGFGSVSGKIEIEIKINHEGEVNRARYMPQNPCIIAT KTPSSDVLVFDYTKHPSKPDPECNPDLRLRGGYGLSWNPN LSGHLLSASDDHTICLWDISAVPGKVVDAKTIFTGHTAVV EDVSWHLLHESLFGSVADDQKLMIWDTRSNNTSKPSHSVD AHTAEVNCLSFNPYSEFILATGSADKTVALWDLRNLKLKL HSFESHKDEIFQVQWSPHNETILASSGTDRRLNVWDLSKI GEEQSPEDAEDGPPELLFIHGGHTAKISDFSWNPNEPWVI CSVSEDNIMQVWQMAENIYND H:  RQAFYLHTTKLTRIARRLCREILRPWHAARHPYLPINSAA IKAECTARLPEVRKPLEAVLRYLETHPR Description Functional site 1) chain B residue 509 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3) source Swiss-Prot : SWS_FT_FI2 2) chain D residue 509 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3) source Swiss-Prot : SWS_FT_FI2 3) chain F residue 509 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3) source Swiss-Prot : SWS_FT_FI2 4) chain H residue 509 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2 and SUMO3) source Swiss-Prot : SWS_FT_FI2 5) chain A residue 355 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 6) chain C residue 355 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 7) chain E residue 355 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 8) chain G residue 355 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 9) chain A residue 193-207 type prosite sequence LLSASDDHTICLWDI description WD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSAsdDhTICLWDI source prosite : PS00678 10) chain A residue 289-303 type prosite sequence LATGSADKTVALWDL description WD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSAsdDhTICLWDI source prosite : PS00678 11) chain A residue 333-347 type prosite sequence LASSGTDRRLNVWDL description WD_REPEATS_1 Trp-Asp (WD) repeats signature. LLSAsdDhTICLWDI source prosite : PS00678 12) chain A residue 160 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 13) chain C residue 160 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 14) chain E residue 160 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 15) chain G residue 160 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI7 16) chain A residue 110 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 17) chain C residue 110 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 18) chain E residue 110 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 19) chain G residue 110 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 160 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q60972 source Swiss-Prot : SWS_FT_FI4 21) chain C residue 160 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q60972 source Swiss-Prot : SWS_FT_FI4 22) chain E residue 160 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q60972 source Swiss-Prot : SWS_FT_FI4 23) chain G residue 160 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q60972 source Swiss-Prot : SWS_FT_FI4

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