eF-site ID 1f66-ABCDEFGHIJ PDB Code 1f66 Chain A, B, C, D, E, F, G, H, I, J click to enlarge Title 2.6 A CRYSTAL STRUCTURE OF A NUCLEOSOME CORE PARTICLE CONTAINING THE VARIANT HISTONE H2A.Z Classification STRUCTURAL PROTEIN/DNA Compound PALINDROMIC 146 BASE PAIR DNA FRAGMENT Source null (1F66) Sequence A:  KKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIA QDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAK RVTIMPKDIQLARRIRGERA B:  RDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFL ENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG C:  AVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSA AILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEE LDSLIKATIAGGGVIPHIHKSLI D:  KTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA VSEGTKAVTKYTSAK E:  GEVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVR EIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAI HAKRVTIMPKDIQLARRIRGERA F:  RHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRG VLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRT LYGFGG G:  AVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSA AILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEE LDSLIKATIAGGGVIPHIHKSLIGKKG H:  KTRKESYAIYVYKVLKQVHPDTGISSKAMSIMNSFVNDVF ERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHA VSEGTKAVTKYTSAK I:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCT GAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT GGTAGAATCTGCAGGTGGATATTGAT J:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCGGAATTCCGCT GAACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTT GGTAGAATCTGCAGGTGGATATTGAT Description Functional site 1) chain D residue 1245 type sequence V description BINDING SITE FOR RESIDUE MN E 1001 source : AC1 2) chain E residue 677 type sequence D description BINDING SITE FOR RESIDUE MN E 1001 source : AC1 3) chain I residue 39 type sequence G description BINDING SITE FOR RESIDUE MN I 1002 source : AC2 4) chain I residue 40 type sequence G description BINDING SITE FOR RESIDUE MN I 1002 source : AC2 5) chain I residue 70 type sequence G description BINDING SITE FOR RESIDUE MN I 1003 source : AC3 6) chain I residue 71 type sequence G description BINDING SITE FOR RESIDUE MN I 1003 source : AC3 7) chain I residue 99 type sequence A description BINDING SITE FOR RESIDUE MN I 1004 source : AC4 8) chain I residue 100 type sequence G description BINDING SITE FOR RESIDUE MN I 1004 source : AC4 9) chain I residue 121 type sequence G description BINDING SITE FOR RESIDUE MN I 1005 source : AC5 10) chain I residue 134 type sequence G description BINDING SITE FOR RESIDUE MN I 1006 source : AC6 11) chain I residue 137 type sequence G description BINDING SITE FOR RESIDUE MN I 1007 source : AC7 12) chain I residue 138 type sequence G description BINDING SITE FOR RESIDUE MN I 1007 source : AC7 13) chain J residue 185 type sequence G description BINDING SITE FOR RESIDUE MN J 1008 source : AC8 14) chain J residue 186 type sequence G description BINDING SITE FOR RESIDUE MN J 1008 source : AC8 15) chain J residue 217 type sequence G description BINDING SITE FOR RESIDUE MN J 1010 source : AC9 16) chain J residue 246 type sequence G description BINDING SITE FOR RESIDUE MN J 1011 source : BC1 17) chain J residue 267 type sequence G description BINDING SITE FOR RESIDUE MN J 1012 source : BC2 18) chain J residue 268 type sequence G description BINDING SITE FOR RESIDUE MN J 1012 source : BC2 19) chain J residue 280 type sequence G description BINDING SITE FOR RESIDUE MN J 1013 source : BC3 20) chain C residue 912 type sequence H description BINDING SITE FOR RESIDUE MN C 1014 source : BC4 21) chain C residue 914 type sequence H description BINDING SITE FOR RESIDUE MN C 1014 source : BC4 22) chain G residue 1112 type sequence H description BINDING SITE FOR RESIDUE MN G 1128 source : BC5 23) chain G residue 1114 type sequence H description BINDING SITE FOR RESIDUE MN G 1128 source : BC5 24) chain A residue 466-474 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 25) chain D residue 1289-1311 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 26) chain A residue 486 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 27) chain E residue 686 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI18 28) chain A residue 515 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 29) chain E residue 715 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI19 30) chain A residue 522 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 31) chain E residue 722 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI20 32) chain A residue 510 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 33) chain E residue 710 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI21 34) chain H residue 1517 type MOD_RES sequence K description 5-glutamyl serotonin; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI4 35) chain F residue 244 type MOD_RES sequence K description Phosphothreonine; by PKC => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI5 36) chain B residue 79 type MOD_RES sequence K description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI8 37) chain F residue 231 type MOD_RES sequence K description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI8 38) chain F residue 277 type MOD_RES sequence K description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI8 39) chain F residue 279 type MOD_RES sequence K description Phosphoserine; alternate; by AURKB, AURKC, RPS6KA3, RPS6KA4 and RPS6KA5 => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI8 40) chain A residue 436 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI10 41) chain A residue 464 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI10 42) chain E residue 636 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI10 43) chain E residue 664 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI10 44) chain A residue 437 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI13 45) chain E residue 637 type MOD_RES sequence K description N6-methyllysine => ECO:0000250|UniProtKB:P68431 source Swiss-Prot : SWS_FT_FI13 46) chain A residue 441 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 47) chain E residue 641 type MOD_RES sequence Y description Phosphotyrosine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI14 48) chain F residue 220 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 49) chain F residue 259 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 50) chain F residue 279 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 51) chain A residue 456 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 52) chain A residue 479 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 53) chain E residue 656 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 54) chain E residue 679 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P84228 source Swiss-Prot : SWS_FT_FI15 55) chain F residue 291 type MOD_RES sequence K description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 56) chain E residue 657 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 57) chain A residue 457 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI16 58) chain E residue 680 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 59) chain E residue 707 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 60) chain A residue 480 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 61) chain A residue 507 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI17 62) chain C residue 823-829 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046

Display surface Download Links