eF-site ID 4wu8-ABCDEFGH PDB Code 4wu8 Chain A, B, C, D, E, F, G, H click to enlarge Title Structure of trPtNAP-NCP145 Classification STRUCTURAL PROTEIN/DNA Compound DNA (145-MER) Source Xenopus laevis (African clawed frog) (H2B11_XENLA) Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV TIMPKDIQLARRIRGE B:  VLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGF GG C:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPKK D:  KTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA VSEGTKAVTKYTSAK E:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV TIMPKDIQLARRIRGE F:  KRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETR GVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGR TLYGFGG G:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPKK H:  KTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA VSEGTKAVTKYTSAK Description Functional site 1) chain C residue 45 type sequence A description binding site for residue SO4 D 201 source : AC3 2) chain C residue 46 type sequence G description binding site for residue SO4 D 201 source : AC3 3) chain C residue 47 type sequence A description binding site for residue SO4 D 201 source : AC3 4) chain D residue 87 type sequence T description binding site for residue SO4 D 201 source : AC3 5) chain D residue 88 type sequence S description binding site for residue SO4 D 201 source : AC3 6) chain D residue 45 type sequence V description binding site for residue MG E 201 source : AC4 7) chain E residue 77 type sequence D description binding site for residue MG E 201 source : AC4 8) chain G residue 44 type sequence G description binding site for residue SO4 H 201 source : AC5 9) chain G residue 45 type sequence A description binding site for residue SO4 H 201 source : AC5 10) chain G residue 46 type sequence G description binding site for residue SO4 H 201 source : AC5 11) chain G residue 47 type sequence A description binding site for residue SO4 H 201 source : AC5 12) chain H residue 87 type sequence T description binding site for residue SO4 H 201 source : AC5 13) chain H residue 88 type sequence S description binding site for residue SO4 H 201 source : AC5 14) chain F residue 47 type CROSSLNK sequence S description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 15) chain C residue 15 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 16) chain C residue 119 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 17) chain G residue 15 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 18) chain G residue 119 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 19) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 20) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 21) chain D residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 22) chain A residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 23) chain E residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 24) chain A residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 25) chain E residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 26) chain A residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 27) chain E residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 28) chain A residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 29) chain E residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 30) chain B residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 31) chain F residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 32) chain B residue 31 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI12 33) chain F residue 31 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI12 34) chain B residue 91 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI13 35) chain F residue 91 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI13 36) chain A residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 37) chain E residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 38) chain A residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 39) chain A residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 40) chain E residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 41) chain E residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 42) chain A residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 43) chain E residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 44) chain A residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 45) chain A residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 46) chain E residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 47) chain E residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 48) chain B residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 49) chain E residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 50) chain F residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 51) chain A residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 52) chain D residue 109 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 53) chain H residue 109 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 54) chain G residue 95 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 55) chain D residue 117 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI4 56) chain G residue 36 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI4 57) chain H residue 117 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI4 58) chain C residue 74 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 59) chain C residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 60) chain G residue 74 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 61) chain G residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 62) chain F residue 16 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 63) chain F residue 44 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 64) chain F residue 79 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 65) chain C residue 104 type MOD_RES sequence Q description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 66) chain G residue 104 type MOD_RES sequence Q description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 67) chain F residue 20 type MOD_RES sequence K description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 68) chain C residue 118 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 69) chain G residue 118 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 70) chain F residue 31 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 71) chain F residue 91 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 72) chain B residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 73) chain B residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 74) chain F residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 75) chain F residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9

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