eF-site ID 4j8u-ABCDEFGH PDB Code 4j8u Chain A, B, C, D, E, F, G, H click to enlarge Title X-ray structure of NCP145 with chlorido(eta-6-p-cymene)(N-phenyl-2-pyridinecarbothioamide)osmium(II) Classification STRUCTURAL PROTEIN/DNA Compound Histone H3.2 Source (4J8U) Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV TIMPKDIQLARRIRGER B:  VLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGF GG C:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPKK D:  KTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA VSEGTKAVTKYTSAK E:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV TIMPKDIQLARRIRGER F:  KRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETR GVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGR TLYGFGG G:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPKK H:  KTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA VSEGTKAVTKYTSAK Description Functional site 1) chain C residue 44 type sequence G description BINDING SITE FOR RESIDUE SO4 D 1101 source : AC1 2) chain C residue 46 type sequence G description BINDING SITE FOR RESIDUE SO4 D 1101 source : AC1 3) chain C residue 47 type sequence A description BINDING SITE FOR RESIDUE SO4 D 1101 source : AC1 4) chain D residue 87 type sequence T description BINDING SITE FOR RESIDUE SO4 D 1101 source : AC1 5) chain D residue 88 type sequence S description BINDING SITE FOR RESIDUE SO4 D 1101 source : AC1 6) chain D residue 89 type sequence R description BINDING SITE FOR RESIDUE SO4 D 1101 source : AC1 7) chain B residue 102 type sequence G description BINDING SITE FOR RESIDUE ELJ D 1102 source : AC2 8) chain D residue 79 type sequence H description BINDING SITE FOR RESIDUE ELJ D 1102 source : AC2 9) chain G residue 37 type sequence G description BINDING SITE FOR RESIDUE ELJ D 1102 source : AC2 10) chain G residue 39 type sequence Y description BINDING SITE FOR RESIDUE ELJ D 1102 source : AC2 11) chain H residue 31 type sequence K description BINDING SITE FOR RESIDUE ELJ D 1102 source : AC2 12) chain H residue 68 type sequence E description BINDING SITE FOR RESIDUE ELJ D 1102 source : AC2 13) chain D residue 45 type sequence V description BINDING SITE FOR RESIDUE MG E 1001 source : AC3 14) chain E residue 77 type sequence D description BINDING SITE FOR RESIDUE MG E 1001 source : AC3 15) chain G residue 44 type sequence G description BINDING SITE FOR RESIDUE SO4 H 201 source : AC4 16) chain G residue 45 type sequence A description BINDING SITE FOR RESIDUE SO4 H 201 source : AC4 17) chain G residue 46 type sequence G description BINDING SITE FOR RESIDUE SO4 H 201 source : AC4 18) chain G residue 47 type sequence A description BINDING SITE FOR RESIDUE SO4 H 201 source : AC4 19) chain H residue 87 type sequence T description BINDING SITE FOR RESIDUE SO4 H 201 source : AC4 20) chain H residue 88 type sequence S description BINDING SITE FOR RESIDUE SO4 H 201 source : AC4 21) chain H residue 46 type sequence H description BINDING SITE FOR RESIDUE SO4 H 202 source : AC5 22) chain H residue 47 type sequence P description BINDING SITE FOR RESIDUE SO4 H 202 source : AC5 23) chain H residue 48 type sequence D description BINDING SITE FOR RESIDUE SO4 H 202 source : AC5 24) chain H residue 49 type sequence T description BINDING SITE FOR RESIDUE SO4 H 202 source : AC5 25) chain G residue 57 type sequence Y description BINDING SITE FOR RESIDUE ELJ H 203 source : AC6 26) chain G residue 61 type sequence E description BINDING SITE FOR RESIDUE ELJ H 203 source : AC6 27) chain G residue 92 type sequence E description BINDING SITE FOR RESIDUE ELJ H 203 source : AC6 28) chain H residue 102 type sequence E description BINDING SITE FOR RESIDUE ELJ H 203 source : AC6 29) chain H residue 106 type sequence H description BINDING SITE FOR RESIDUE ELJ H 203 source : AC6 30) chain C residue 36 type sequence K description BINDING SITE FOR RESIDUE ELJ H 204 source : AC7 31) chain C residue 37 type sequence G description BINDING SITE FOR RESIDUE ELJ H 204 source : AC7 32) chain C residue 39 type sequence Y description BINDING SITE FOR RESIDUE ELJ H 204 source : AC7 33) chain D residue 68 type sequence E description BINDING SITE FOR RESIDUE ELJ H 204 source : AC7 34) chain F residue 84 type sequence M description BINDING SITE FOR RESIDUE ELJ H 204 source : AC7 35) chain F residue 88 type sequence Y description BINDING SITE FOR RESIDUE ELJ H 204 source : AC7 36) chain H residue 79 type sequence H description BINDING SITE FOR RESIDUE ELJ H 204 source : AC7 37) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 38) chain D residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 39) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 40) chain B residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 41) chain E residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 42) chain F residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 43) chain A residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 44) chain B residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 45) chain F residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 46) 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 47) 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 48) 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 49) 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 50) chain A residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 51) chain E residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 52) chain A residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 53) chain A residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 54) chain E residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 55) chain E residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 56) chain A residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 57) chain E residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 58) chain A residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 59) chain A residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 60) chain E residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 61) chain E residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 62) chain A residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 63) chain E residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 64) chain A residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 65) chain E residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 66) chain A residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 67) chain E residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 68) chain A residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 69) chain E residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 70) chain D residue 109 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 71) chain H residue 109 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 72) chain G residue 95 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 73) 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 74) 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 75) 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 76) chain C residue 74 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 77) chain C residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 78) chain G residue 74 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 79) chain G residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 80) chain F residue 16 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 81) chain F residue 44 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 82) chain F residue 79 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 83) chain C residue 104 type MOD_RES sequence Q description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 84) chain G residue 104 type MOD_RES sequence Q description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 85) chain F residue 20 type MOD_RES sequence K description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 86) chain C residue 118 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 87) chain G residue 118 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 88) chain F residue 31 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 89) chain F residue 91 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 90) 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 91) 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 92) 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 93) 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 94) 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 95) chain B residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 96) chain B residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 97) chain F residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 98) 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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