eF-site ID 6r8y-ABCDEFGHIJKL PDB Code 6r8y Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title Cryo-EM structure of NCP-6-4PP(-1)-UV-DDB Classification DNA BINDING PROTEIN Compound Histone H3.1 Source (DDB2_HUMAN) Sequence A:  VKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREI AQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHA KRVTIMPKDIQLARRIRGERA B:  RHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRG VLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRT LYGFGG C:  KARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAP VYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIR NDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHK D:  RKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVND IFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAK HAVSEGTKAVTKYTSAK E:  VKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREI AQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHA KRVTIMPKDIQLARRIRGERA F:  VLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGF GG G:  KARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAP VYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIR NDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHK H:  RKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVND IFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAK HAVSEGTKAVTKYTSAK I:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG AAACTGCTCAATCAAAAGGCATGTTCAGCTGGTTCAGCTG AACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTG GTAGAATCTGCAGGTGGATATTGAT J:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGAACCAGCTG AACATGCCTTTTGAXGAGCAGTTTCCAAATACACTTTTGG TAGAATCTGCAGGTGGATATTGAT K:  MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLE IYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGI IGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREK EFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRL FMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIV DMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGKLHIRTV PLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPS ASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLIID QHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAM VYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMVE FNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLK TKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWMS AVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEV GLFHLGEFVNVFCHGSLVMQNLGETSTPTQGSVLFGTVNG MIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRS FHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQYD DGSGMKREATADDLIKVVEELTRIH L:  VGLAGPQILPPCRSIVRTLHQHKLGRASWPSVQQGLQQSF LHTLDSYRILQKAAPFDRRATSLAWHPTHPSTVAVGSKGG DIMLWNFGIKDKPTFIKGIGAGGSITGLKFNPLNTNQFYA SSMEGTTRLQDFKGNILRVFASSDTINIWFCSLDVSASSR MVVTGDNVGNVILLNMDGKELWNLRMHKKKVTHVALNPCC DWFLATASVDQTVKIWDLRQVRGKASFLYSLPHRHPVNAA CFSPDGARLLTTDQKSEIRVYSASQWDCPLGLIPHPHRHF QHLTPIKAAWHPRYNLIVVGRYPDPNFKSCTPYELRTIDV FDGNSGKMMCQLYDPESSGISSLNEFNPMGDTLASAMGYH ILIWSQEEARTRK Description (1)  Histone H3.1, Histone H4, Histone H2A type 1-B/E, Histone H2B type 1-J, DNA damage-binding protein 1, DNA damage-binding protein 2/DNA Complex Functional site 1) chain F residue 60 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI16 2) chain F residue 80 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI16 3) chain F residue 32 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in UFM1); alternate => ECO:0000269|PubMed:30886146 source Swiss-Prot : SWS_FT_FI17 4) chain A residue 38 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 5) chain H residue 121 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 6) chain D residue 121 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 7) chain D residue 35 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 8) chain H residue 35 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 9) chain A residue 80 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711 source Swiss-Prot : SWS_FT_FI21 10) chain E residue 80 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711 source Swiss-Prot : SWS_FT_FI21 11) chain A residue 81 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI22 12) chain E residue 81 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI22 13) chain A residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI23 14) chain E residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI23 15) chain A residue 108 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI24 16) chain E residue 108 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI24 17) chain A residue 116 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI25 18) chain E residue 116 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI25 19) chain A residue 123 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229 source Swiss-Prot : SWS_FT_FI26 20) chain E residue 123 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229 source Swiss-Prot : SWS_FT_FI26 21) chain L residue 258-272 type prosite sequence LATASVDQTVKIWDL description WD_REPEATS_1 Trp-Asp (WD) repeats signature. LATAsvDqTVKIWDL source prosite : PS00678 22) chain D residue 93-115 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 23) chain A residue 67-75 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 24) chain C residue 22-28 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 25) chain G residue 75 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:27338793 source Swiss-Prot : SWS_FT_FI7 26) chain G residue 76 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:12086618, ECO:0000269|PubMed:15964846, ECO:0000269|PubMed:17967882, ECO:0000269|PubMed:27338793 source Swiss-Prot : SWS_FT_FI7 27) chain H residue 44 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:32789493 source Swiss-Prot : SWS_FT_FI3 28) chain H residue 86 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:32789493 source Swiss-Prot : SWS_FT_FI3 29) chain D residue 44 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:32789493 source Swiss-Prot : SWS_FT_FI3 30) chain D residue 86 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:32789493 source Swiss-Prot : SWS_FT_FI3 31) chain L residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:32789493 source Swiss-Prot : SWS_FT_FI3 32) chain K residue 1121 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI4 33) chain G residue 10 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI4 34) chain G residue 96 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733 source Swiss-Prot : SWS_FT_FI4 35) chain F residue 45 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393 source Swiss-Prot : SWS_FT_FI5 36) chain F residue 32 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI6 37) chain F residue 78 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI6 38) chain F residue 92 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI6 39) chain H residue 117 type MOD_RES sequence K description Phosphoserine; by PAK2 => ECO:0000269|PubMed:21724829, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 40) chain H residue 121 type MOD_RES sequence K description Phosphoserine; by PAK2 => ECO:0000269|PubMed:21724829, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 41) chain F residue 48 type MOD_RES sequence S description Phosphoserine; by PAK2 => ECO:0000269|PubMed:21724829, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 42) chain D residue 117 type MOD_RES sequence K description Phosphoserine; by PAK2 => ECO:0000269|PubMed:21724829, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 43) chain D residue 121 type MOD_RES sequence K description Phosphoserine; by PAK2 => ECO:0000269|PubMed:21724829, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 44) chain H residue 35 type MOD_RES sequence K description Phosphoserine; by PAK2 => ECO:0000269|PubMed:21724829, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI8 45) chain F residue 52 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI9 46) chain H residue 36 type MOD_RES sequence E description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI9 47) chain C residue 126 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI9 48) chain G residue 119 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI9 49) chain G residue 120 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI9 50) chain G residue 126 type MOD_RES sequence K description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI9 51) chain E residue 57 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI10 52) chain F residue 60 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI10 53) chain H residue 37 type MOD_RES sequence S description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI10 54) chain F residue 80 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806 source Swiss-Prot : SWS_FT_FI11 55) chain D residue 109 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806 source Swiss-Prot : SWS_FT_FI11 56) chain H residue 47 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806 source Swiss-Prot : SWS_FT_FI11 57) chain H residue 109 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806 source Swiss-Prot : SWS_FT_FI11 58) chain F residue 81 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P62806 source Swiss-Prot : SWS_FT_FI12 59) chain H residue 58 type MOD_RES sequence K description Phosphothreonine => ECO:0000250|UniProtKB:P62806 source Swiss-Prot : SWS_FT_FI12 60) chain G residue 120 type MOD_RES sequence K description Phosphothreonine => ECO:0000250|UniProtKB:P62806 source Swiss-Prot : SWS_FT_FI12 61) chain F residue 89 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI13 62) chain H residue 80 type MOD_RES sequence R description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI13 63) chain H residue 87 type CROSSLNK sequence R description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447 source Swiss-Prot : SWS_FT_FI14 64) chain H residue 93 type CROSSLNK sequence R description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447 source Swiss-Prot : SWS_FT_FI14 65) chain D residue 93 type CROSSLNK sequence R description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:25218447 source Swiss-Prot : SWS_FT_FI14 66) chain D residue 116 type CROSSLNK sequence T description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:19818714 source Swiss-Prot : SWS_FT_FI15 67) chain F residue 92 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:19818714 source Swiss-Prot : SWS_FT_FI15

Display surface Download Links