eF-site ID 3mgp-ABCDEFGHIJ PDB Code 3mgp Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title Binding of Cobalt ions to the Nucleosome Core Particle Classification STRUCTURAL PROTEIN/DNA Compound Histone H3.2 Source (3MGP) Sequence A:  KPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQ DFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKR VTIMPKDIQLARRIRGERA B:  DNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLE NVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG C:  KTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAV LEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEELN KLLGRVTIAQGGVLPNIQSVLLPK D:  GKKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSF VNDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGE LAKHAVSEGTKAVTKYTSAK E:  KPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQ DFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKR VTIMPKDIQLARRIRGERA F:  KRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETR GVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGR TLYGFGG G:  KAKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLA AVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAVRNDEE LNKLLGRVTIAQGGVLPNIQSVLLPK H:  KKRRKTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFV NDVFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGEL AKHAVSEGTKAVTKYTSAK I:  ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGGAATCCAGC TGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTT TGGTAGTATCTGCAGGTGGATATTGAT J:  ATCAATATCCACCTGCAGATACTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGGATTCCAGC TGAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTT TGGTAGTATCTGCAGGTGGATATTGAT Description Functional site 1) chain D residue 45 type sequence V description BINDING SITE FOR RESIDUE CO E 136 source : AC1 2) chain E residue 77 type sequence D description BINDING SITE FOR RESIDUE CO E 136 source : AC1 3) chain J residue 27 type sequence G description BINDING SITE FOR RESIDUE CO J 74 source : AC2 4) chain I residue 61 type sequence G description BINDING SITE FOR RESIDUE CO I 74 source : AC3 5) chain J residue 61 type sequence G description BINDING SITE FOR RESIDUE CO J 75 source : AC4 6) chain J residue 62 type sequence G description BINDING SITE FOR RESIDUE CO J 75 source : AC4 7) chain I residue 47 type sequence T description BINDING SITE FOR RESIDUE CO I 75 source : AC5 8) chain I residue 48 type sequence G description BINDING SITE FOR RESIDUE CO I 75 source : AC5 9) chain J residue 48 type sequence G description BINDING SITE FOR RESIDUE CO J 76 source : AC6 10) chain J residue -3 type sequence G description BINDING SITE FOR RESIDUE CO J 77 source : AC7 11) chain I residue 27 type sequence G description BINDING SITE FOR RESIDUE CO I 76 source : AC8 12) chain I residue -3 type sequence G description BINDING SITE FOR RESIDUE CO I 77 source : AC9 13) chain D residue 102 type sequence E description BINDING SITE FOR RESIDUE CO D 123 source : BC1 14) chain D residue 106 type sequence H description BINDING SITE FOR RESIDUE CO D 123 source : BC1 15) chain F residue 18 type sequence H description BINDING SITE FOR RESIDUE CO D 123 source : BC1 16) chain J residue -6 type sequence G description BINDING SITE FOR RESIDUE CO J 78 source : BC2 17) chain I residue -35 type sequence G description BINDING SITE FOR RESIDUE CO I 78 source : BC3 18) chain I residue -34 type sequence G description BINDING SITE FOR RESIDUE CO I 78 source : BC3 19) chain J residue -35 type sequence G description BINDING SITE FOR RESIDUE CO J 79 source : BC4 20) chain J residue -34 type sequence G description BINDING SITE FOR RESIDUE CO J 79 source : BC4 21) chain H residue 79 type sequence H description BINDING SITE FOR RESIDUE CO H 123 source : BC5 22) chain H residue 105 type sequence K description BINDING SITE FOR RESIDUE CO H 124 source : BC6 23) chain H residue 106 type sequence H description BINDING SITE FOR RESIDUE CO H 124 source : BC6 24) chain J residue 29 type sequence A description BINDING SITE FOR RESIDUE CO J 80 source : BC7 25) chain J residue -56 type sequence G description BINDING SITE FOR RESIDUE CO J 81 source : BC8 26) chain I residue 14 type sequence G description BINDING SITE FOR RESIDUE CO I 79 source : BC9 27) chain I residue 16 type sequence C description BINDING SITE FOR RESIDUE CO I 79 source : BC9 28) chain J residue -14 type sequence C description BINDING SITE FOR RESIDUE CO I 79 source : BC9 29) chain J residue -15 type sequence G description BINDING SITE FOR RESIDUE CO I 79 source : BC9 30) chain I residue -56 type sequence G description BINDING SITE FOR RESIDUE CO I 80 source : CC1 31) chain J residue 8 type sequence G description BINDING SITE FOR RESIDUE CO J 82 source : CC2 32) chain J residue 5 type sequence G description BINDING SITE FOR RESIDUE CO J 83 source : CC3 33) chain J residue 71 type sequence G description BINDING SITE FOR RESIDUE CO J 84 source : CC4 34) chain J residue 52 type sequence G description BINDING SITE FOR RESIDUE CO J 85 source : CC5 35) chain I residue 24 type sequence G description BINDING SITE FOR RESIDUE CO I 81 source : CC6 36) chain I residue 25 type sequence G description BINDING SITE FOR RESIDUE CO I 81 source : CC6 37) chain I residue 65 type sequence G description BINDING SITE FOR RESIDUE CO I 82 source : CC7 38) chain D residue 79 type sequence H description BINDING SITE FOR RESIDUE CO D 124 source : CC8 39) chain C residue 90 type sequence D description BINDING SITE FOR RESIDUE CO C 120 source : CC9 40) chain I residue 59 type sequence C description BINDING SITE FOR RESIDUE CO I 84 source : DC1 41) chain J residue -59 type sequence G description BINDING SITE FOR RESIDUE CO I 84 source : DC1 42) chain J residue -34 type sequence G description BINDING SITE FOR RESIDUE CO J 88 source : DC2 43) chain J residue 64 type sequence G description BINDING SITE FOR RESIDUE CO J 89 source : DC3 44) chain J residue 65 type sequence G description BINDING SITE FOR RESIDUE CO J 89 source : DC3 45) chain I residue 29 type sequence A description BINDING SITE FOR RESIDUE CO I 85 source : DC4 46) chain I residue 64 type sequence G description BINDING SITE FOR RESIDUE CO I 86 source : DC5 47) chain J residue 25 type sequence G description BINDING SITE FOR RESIDUE CO J 90 source : DC7 48) chain J residue -1 type sequence A description BINDING SITE FOR RESIDUE CO J 91 source : DC8 49) chain I residue 71 type sequence G description BINDING SITE FOR RESIDUE CO I 89 source : DC9 50) chain I residue -6 type sequence G description BINDING SITE FOR RESIDUE CO I 94 source : EC1 51) chain J residue 23 type sequence T description BINDING SITE FOR RESIDUE CO J 102 source : EC2 52) chain J residue 24 type sequence G description BINDING SITE FOR RESIDUE CO J 102 source : EC2 53) chain G residue 44 type sequence G description BINDING SITE FOR RESIDUE CL G 3145 source : EC3 54) chain G residue 46 type sequence G description BINDING SITE FOR RESIDUE CL G 3145 source : EC3 55) chain G residue 47 type sequence A description BINDING SITE FOR RESIDUE CL G 3145 source : EC3 56) chain H residue 87 type sequence T description BINDING SITE FOR RESIDUE CL G 3145 source : EC3 57) chain H residue 88 type sequence S description BINDING SITE FOR RESIDUE CL G 3145 source : EC3 58) chain C residue 46 type sequence G description BINDING SITE FOR RESIDUE CL D 3146 source : EC4 59) chain C residue 47 type sequence A description BINDING SITE FOR RESIDUE CL D 3146 source : EC4 60) chain D residue 87 type sequence T description BINDING SITE FOR RESIDUE CL D 3146 source : EC4 61) chain D residue 88 type sequence S description BINDING SITE FOR RESIDUE CL D 3146 source : EC4 62) chain A residue 121 type sequence P description BINDING SITE FOR RESIDUE CL A 3147 source : EC5 63) chain A residue 122 type sequence K description BINDING SITE FOR RESIDUE CL A 3147 source : EC5 64) chain E residue 121 type sequence P description BINDING SITE FOR RESIDUE CL E 3148 source : EC6 65) chain E residue 122 type sequence K description BINDING SITE FOR RESIDUE CL E 3148 source : EC6 66) chain A residue 37 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 67) 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 68) 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 69) 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 70) 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 71) chain A residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 72) chain E residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 73) chain A residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 74) chain E residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 75) chain A residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 76) chain E residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 77) chain A residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 78) chain E residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 79) chain B residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 80) chain E residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 81) chain F residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 82) chain A residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 83) chain B residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 84) chain F residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 85) 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 86) 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 87) chain A residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 88) chain E residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 89) chain A residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 90) chain A residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 91) chain E residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 92) chain E residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 93) chain A residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 94) chain A residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 95) chain E residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 96) chain E residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 97) chain D residue 109 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 98) chain H residue 109 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 99) chain B residue 44 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 100) chain B residue 79 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 101) chain F residue 16 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 102) chain F residue 44 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 103) chain F residue 79 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 104) chain F residue 20 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 105) chain B residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 106) chain B residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 107) chain F residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 108) chain F residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 109) chain B residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 110) chain F residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 111) chain B residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 112) chain B residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 113) chain F residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 114) chain F residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 115) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 116) chain D residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 117) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 118) chain A residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 119) chain E residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16

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