eF-site ID 3mgp-ABCDEFGH PDB Code 3mgp Chain A, B, C, D, E, F, G, H 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 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 D residue 102 type sequence E description BINDING SITE FOR RESIDUE CO D 123 source : BC1 4) chain D residue 106 type sequence H description BINDING SITE FOR RESIDUE CO D 123 source : BC1 5) chain F residue 18 type sequence H description BINDING SITE FOR RESIDUE CO D 123 source : BC1 6) chain H residue 79 type sequence H description BINDING SITE FOR RESIDUE CO H 123 source : BC5 7) chain H residue 105 type sequence K description BINDING SITE FOR RESIDUE CO H 124 source : BC6 8) chain H residue 106 type sequence H description BINDING SITE FOR RESIDUE CO H 124 source : BC6 9) chain D residue 79 type sequence H description BINDING SITE FOR RESIDUE CO D 124 source : CC8 10) chain C residue 90 type sequence D description BINDING SITE FOR RESIDUE CO C 120 source : CC9 11) chain G residue 44 type sequence G description BINDING SITE FOR RESIDUE CL G 3145 source : EC3 12) chain G residue 46 type sequence G description BINDING SITE FOR RESIDUE CL G 3145 source : EC3 13) chain G residue 47 type sequence A description BINDING SITE FOR RESIDUE CL G 3145 source : EC3 14) chain H residue 87 type sequence T description BINDING SITE FOR RESIDUE CL G 3145 source : EC3 15) chain H residue 88 type sequence S description BINDING SITE FOR RESIDUE CL G 3145 source : EC3 16) chain C residue 46 type sequence G description BINDING SITE FOR RESIDUE CL D 3146 source : EC4 17) chain C residue 47 type sequence A description BINDING SITE FOR RESIDUE CL D 3146 source : EC4 18) chain D residue 87 type sequence T description BINDING SITE FOR RESIDUE CL D 3146 source : EC4 19) chain D residue 88 type sequence S description BINDING SITE FOR RESIDUE CL D 3146 source : EC4 20) chain A residue 121 type sequence P description BINDING SITE FOR RESIDUE CL A 3147 source : EC5 21) chain A residue 122 type sequence K description BINDING SITE FOR RESIDUE CL A 3147 source : EC5 22) chain E residue 121 type sequence P description BINDING SITE FOR RESIDUE CL E 3148 source : EC6 23) chain E residue 122 type sequence K description BINDING SITE FOR RESIDUE CL E 3148 source : EC6 24) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 25) chain D residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 26) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 27) chain B residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 28) chain E residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 29) chain F residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 30) chain A residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 31) chain B residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 32) chain F residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 33) 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 34) 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 35) 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 36) 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 37) 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 38) chain A residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 39) chain E residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 40) chain A residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 41) chain A residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 42) chain E residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 43) chain E residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 44) chain A residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 45) chain E residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 46) chain A residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 47) chain A residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 48) chain E residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 49) chain E residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 50) chain A residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 51) chain E residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 52) chain A residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 53) chain E residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 54) chain A residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 55) chain E residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 56) chain A residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 57) chain E residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 58) chain D residue 109 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 59) chain H residue 109 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 60) 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 61) 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 62) chain B residue 44 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 63) chain B residue 79 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 64) chain F residue 16 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 65) chain F residue 44 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 66) chain F residue 79 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 67) chain F residue 20 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 68) chain B residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 69) chain B residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 70) chain F residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 71) chain F residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 72) chain B residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 73) chain F residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 74) chain B residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 75) chain B residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 76) chain F residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 77) 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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