eF-site ID 5ay8-ABCDEFGHIJ PDB Code 5ay8 Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title Crystal structure of human nucleosome containing H3.Y Classification DNA BINDING PROTEIN/DNA Compound H3.Y Source (5AY8) Sequence A:  PHRYKPGTLALREIRKYQKSTQLLLRKLPFQRLVREIAQA ISPDLRFQSAAIGALQEASEAYLVQLFEDTNLCAIHARRV TIMPRDMQLARRLRREG B:  NIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLEN VIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG C:  AKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAA VLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEEL NKLLGRVTIAQGGVLPNIQAVLLPK D:  RKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFER IAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVS EGTKAVTKYTSA E:  PHRYKPGTLALREIRKYQKSTQLLLRKLPFQRLVREIAQA ISPDLRFQSAAIGALQEASEAYLVQLFEDTNLCAIHARRV TIMPRDMQLARRLRRE F:  DNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLE NVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG G:  KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAV LEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELN KLLGRVTIAQGGVLPNIQAVLLPK H:  RKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFER IAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVS EGTKAVTKYTSA I:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGAATTCAGCT GAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT GGTAGAATCTGCAGGTGGATATTGA J:  TCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGGA AACTGCTCCATCAAAAGGCATGTTCAGCTGAATTCAGCTG AACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTG GTAGAATCTGCAGGTGGATATTGAT Description Functional site 1) chain A residue 63 type sequence R description binding site for residue MN A 201 source : AC1 2) chain B residue 28 type sequence G description binding site for residue MN A 201 source : AC1 3) chain B residue 30 type sequence T description binding site for residue MN A 201 source : AC1 4) chain B residue 33 type sequence A description binding site for residue MN A 201 source : AC1 5) chain G residue 45 type sequence A description binding site for residue MN G 201 source : AC2 6) chain G residue 46 type sequence G description binding site for residue MN G 201 source : AC2 7) chain G residue 47 type sequence A description binding site for residue MN G 201 source : AC2 8) chain H residue 90 type sequence T description binding site for residue MN G 201 source : AC2 9) chain H residue 91 type sequence S description binding site for residue MN G 201 source : AC2 10) chain I residue 15 type sequence G description binding site for residue MN I 202 source : AC3 11) chain I residue 16 type sequence C description binding site for residue MN I 202 source : AC3 12) chain J residue 283 type sequence G description binding site for residue MN J 301 source : AC4 13) chain J residue 283 type sequence G description binding site for residue MN J 302 source : AC5 14) chain J residue 280 type sequence G description binding site for residue MN J 303 source : AC6 15) chain J residue 246 type sequence G description binding site for residue MN J 304 source : AC7 16) chain J residue 290 type sequence G description binding site for residue CL J 305 source : AC8 17) chain J residue 218 type sequence A description binding site for residue CL J 306 source : AC9 18) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 19) chain D residue 92-114 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 20) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 21) chain A residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI10 22) chain E residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI10 23) chain D residue 46 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 24) chain D residue 108 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 25) chain H residue 46 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 26) chain H residue 108 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 27) chain D residue 57 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI12 28) chain H residue 57 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI12 29) chain D residue 79 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 30) chain H residue 79 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 31) chain D residue 86 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 32) chain D residue 92 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 33) chain H residue 86 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 34) chain H residue 92 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 35) chain D residue 115 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 36) chain H residue 115 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 37) chain F residue 91 type MOD_RES sequence K description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 38) chain D residue 112 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 39) chain H residue 112 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 40) chain B residue 79 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 41) chain F residue 59 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 42) chain F residue 79 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 43) chain D residue 120 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563 source Swiss-Prot : SWS_FT_FI18 44) chain H residue 120 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:16307923, ECO:0000269|PubMed:16627869, ECO:0000269|PubMed:16713563 source Swiss-Prot : SWS_FT_FI18 45) chain D residue 34 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816 source Swiss-Prot : SWS_FT_FI20 46) chain H residue 34 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:21726816 source Swiss-Prot : SWS_FT_FI20 47) chain E residue 64 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI3 48) chain H residue 43 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI3 49) chain H residue 85 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI3 50) chain A residue 64 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI3 51) chain G residue 95 type MOD_RES sequence K description 5-glutamyl serotonin; alternate => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI4 52) chain B residue 44 type MOD_RES sequence K description Symmetric dimethylarginine => ECO:0000250|UniProtKB:P84244 source Swiss-Prot : SWS_FT_FI5 53) chain F residue 44 type MOD_RES sequence K description Symmetric dimethylarginine => ECO:0000250|UniProtKB:P84244 source Swiss-Prot : SWS_FT_FI5 54) chain B residue 77 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI6 55) chain B residue 91 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI6 56) chain F residue 31 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI6 57) chain F residue 77 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI6 58) chain F residue 91 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI6 59) chain A residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI7 60) chain E residue 41 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI7 61) chain G residue 74 type MOD_RES sequence K description Phosphotyrosine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI7 62) chain G residue 75 type MOD_RES sequence K description Phosphotyrosine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI7 63) chain A residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI8 64) chain E residue 56 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI8 65) chain D residue 120 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI8 66) chain H residue 34 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI8 67) chain H residue 116 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI8 68) chain H residue 120 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI8 69) chain A residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI9 70) chain A residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI9 71) chain E residue 57 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI9 72) chain E residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI9

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