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 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 25) 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 26) 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 27) 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 28) 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 29) chain A residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 30) chain E residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 31) chain A residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 32) chain E residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 33) chain A residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 34) chain E residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 35) chain A residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 36) chain E residue 110 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 37) chain B residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 38) chain E residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 39) chain F residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 40) chain A residue 64 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI10 41) chain B residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 42) chain F residue 77 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI11 43) 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 44) 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 45) chain A residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 46) chain E residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 47) chain A residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 48) chain A residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 49) chain E residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 50) chain E residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 51) chain A residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 52) chain A residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 53) chain E residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 54) chain E residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 55) chain D residue 109 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 56) chain H residue 109 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI3 57) chain B residue 44 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 58) chain B residue 79 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 59) chain F residue 16 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 60) chain F residue 44 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 61) chain F residue 79 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI5 62) chain F residue 20 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI6 63) chain B residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 64) chain B residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 65) chain F residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 66) chain F residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI7 67) chain B residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 68) chain F residue 47 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI8 69) chain B residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 70) chain B residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 71) chain F residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 72) chain F residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P62805 source Swiss-Prot : SWS_FT_FI9 73) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 74) chain D residue 89-111 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 75) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 76) chain A residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 77) 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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