eF-site ID 1kx4-ABCDEFGHIJ PDB Code 1kx4 Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title X-Ray Structure of the Nucleosome Core Particle, NCP146b, at 2.6 A Resolution Classification STRUCTURAL PROTEIN/DNA Compound DNA (5'(ATCTCCAAATATCCCTTGCGGATCGTAGAAAAAGTGTGTCAAACTGCGCTATCAAAGGGAAACTTCAACTGAATTCAGTTGAAGTTTCCCTTTGATAGCGCAGTTTGACACACTTTTTCTACGATCCGCAAGGGATATTTGGAGAT)3') Source Bos taurus (Bovine) (1KX4) Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRV TIMPKDIQLARRIRGERA B:  KVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLK VFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYG FGG C:  TRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVL EYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELNK LLGRVTIAQGGVLPNIQSVLLPK D:  KKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFV NDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGEL AKHAVSEGTKAVTKYTSAK E:  HRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDF KTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVT IMPKDIQLARRIRGERA F:  NIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLEN VIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG G:  AKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEEL NKLLGRVTIAQGGVLPNIQSVLLPK H:  TRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSAK I:  ATCTCCAAATATCCCTTGCGGATCGTAGAAAAAGTGTGTC AAACTGCGCTATCAAAGGGAAACTTCAACTGAATTCAGTT GAAGTTTCCCTTTGATAGCGCAGTTTGACACACTTTTTCT ACGATCCGCAAGGGATATTTGGAGAT J:  ATCTCCAAATATCCCTTGCGGATCGTAGAAAAAGTGTGTC AAACTGCGCTATCAAAGGGAAACTTCAACTGAATTCAGTT GAAGTTTCCCTTTGATAGCGCAGTTTGACACACTTTTTCT ACGATCCGCAAGGGATATTTGGAGAT Description Functional site 1) chain A residue 77 type sequence D description BINDING SITE FOR RESIDUE MN A 434 source : AC1 2) chain H residue 45 type sequence V description BINDING SITE FOR RESIDUE MN A 434 source : AC1 3) chain E residue 81 type sequence D description BINDING SITE FOR RESIDUE MN J 435 source : AC2 4) chain J residue 66 type sequence T description BINDING SITE FOR RESIDUE MN J 435 source : AC2 5) chain I residue -53 type sequence G description BINDING SITE FOR RESIDUE MN I 436 source : AC3 6) chain I residue 68 type sequence G description BINDING SITE FOR RESIDUE MN I 437 source : AC4 7) chain I residue 69 type sequence G description BINDING SITE FOR RESIDUE MN I 437 source : AC4 8) chain I residue 27 type sequence G description BINDING SITE FOR RESIDUE MN I 438 source : AC5 9) chain I residue -14 type sequence G description BINDING SITE FOR RESIDUE MN I 439 source : AC6 10) chain G residue 46 type sequence G description BINDING SITE FOR RESIDUE CL G 440 source : AC7 11) chain G residue 47 type sequence A description BINDING SITE FOR RESIDUE CL G 440 source : AC7 12) chain H residue 87 type sequence T description BINDING SITE FOR RESIDUE CL G 440 source : AC7 13) chain H residue 88 type sequence S description BINDING SITE FOR RESIDUE CL G 440 source : AC7 14) chain C residue 46 type sequence G description BINDING SITE FOR RESIDUE CL C 441 source : AC8 15) chain D residue 87 type sequence T description BINDING SITE FOR RESIDUE CL C 441 source : AC8 16) chain D residue 88 type sequence S description BINDING SITE FOR RESIDUE CL C 441 source : AC8 17) chain A residue 122 type sequence K description BINDING SITE FOR RESIDUE CL A 442 source : AC9 18) chain E residue 122 type sequence K description BINDING SITE FOR RESIDUE CL E 443 source : BC1 19) chain A residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 20) chain E residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 21) chain A residue 116 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 22) chain E residue 116 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 23) chain A residue 123 type MOD_RES sequence D description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 24) chain E residue 123 type MOD_RES sequence D description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 25) chain A residue 111 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 26) chain E residue 111 type LIPID sequence A description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 27) chain C residue 105 type MOD_RES sequence G description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 28) chain G residue 105 type MOD_RES sequence G description N5-methylglutamine => ECO:0000250 source Swiss-Prot : SWS_FT_FI6 29) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 30) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 31) chain D residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 32) chain B residue 60 type MOD_RES sequence V description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 33) chain F residue 60 type MOD_RES sequence V description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 34) chain B residue 78 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 35) chain F residue 78 type MOD_RES sequence R description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 36) chain B residue 32 type CROSSLNK sequence P description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI12 37) chain F residue 32 type CROSSLNK sequence P description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI12 38) chain B residue 92 type CROSSLNK sequence R description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI13 39) chain F residue 92 type CROSSLNK sequence R description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI13 40) chain A residue 38 type MOD_RES sequence P description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI14 41) chain A residue 42 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI15 42) chain E residue 42 type MOD_RES sequence R description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI15 43) chain A residue 58 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 44) chain E residue 58 type MOD_RES sequence T description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 45) chain A residue 81 type MOD_RES sequence D description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 46) chain A residue 108 type MOD_RES sequence N description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 47) chain E residue 81 type MOD_RES sequence D description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 48) chain E residue 108 type MOD_RES sequence N description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 49) chain D residue 110 type CARBOHYD sequence E description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 50) chain H residue 110 type CARBOHYD sequence E description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 51) chain G residue 96 type CARBOHYD sequence L description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 52) chain D residue 118 type CROSSLNK sequence Y description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI4 53) chain G residue 37 type CROSSLNK sequence G description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI4 54) chain H residue 118 type CROSSLNK sequence Y description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:P0C1H4 source Swiss-Prot : SWS_FT_FI4 55) chain C residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 56) chain E residue 65 type MOD_RES sequence L description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 57) chain C residue 76 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 58) chain G residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 59) chain G residue 76 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 60) chain F residue 45 type MOD_RES sequence R description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 61) chain F residue 80 type MOD_RES sequence T description N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI5 62) chain F residue 32 type MOD_RES sequence P description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 63) chain F residue 92 type MOD_RES sequence R description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P0C0S8 source Swiss-Prot : SWS_FT_FI7 64) chain F residue 48 type CROSSLNK sequence G description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 65) chain C residue 16 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 66) chain G residue 14 type CROSSLNK sequence A description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 67) chain G residue 16 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250 source Swiss-Prot : SWS_FT_FI8 68) chain B residue 52 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 69) chain B residue 89 type MOD_RES sequence A description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 70) chain F residue 52 type MOD_RES sequence E description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 71) chain F residue 89 type MOD_RES sequence A description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9

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