eF-site ID 6r91-ABCDEFGHIJKL PDB Code 6r91 Chain A, B, C, D, E, F, G, H, I, J, K, L click to enlarge Title Cryo-EM structure of NCP_THF2(-3)-UV-DDB Classification DNA BINDING PROTEIN Compound Histone H3.1 Source (DDB2_HUMAN) Sequence A:  VKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREI AQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHA KRVTIMPKDIQLARRIRGERA B:  LRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVF LENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFG G C:  ARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPV YLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRN DEELNKLLGRVTIAQGGVLPNIQAVLLPKK D:  RKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVND IFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAK HAVSEGTKAVTKYTSAK E:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRV TIMPKDIQLARRIRGERA F:  VLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGF GG G:  KARAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAP VYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIR NDEELNKLLGRVTIAQGGVLPNIQAVLLPKK H:  RKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVND IFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAK HAVSEGTKAVTKYTSAK I:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGGTTCAGCTG AACATGCCTTTTGATGGAGCAGTTTCCAAATACACTTTTG GTAGAATCTGCAGGTGGATATTGAT J:  ATCAATATCCACCTGCAGATTCTACCAAAAGTGTATTTGG AAACTGCTCCATCAAAAGGCATGTTCAGCTGAACCAGCTG AACATGCCTTTTGATGXXGCAGTTTCCAAATACACTTTTG GTAGAATCTGCAGGTGGATATTGAT K:  MSYNYVVTAQKPTAVNGCVTGHFTSAEDLNLLIAKNTRLE IYVVTAEGLRPVKEVGMYGKIAVMELFRPKGESKDLLFIL TAKYNACILEYKQSGESIDIITRAHGNVQDRIGRPSETGI IGIIDPECRMIGLRLYDGLFKVIPLDRDNKELKAFNIRLE ELHVIDVKFLYGCQAPTICFVYQDPQGRHVKTYEVSLREK EFNKGPWKQENVEAEASMVIAVPEPFGGAIIIGQESITYH NGDKYLAIAPPIIKQSTIVCHNRVDPNGSRYLLGDMEGRL FMLLLEKEEQMDGTVTLKDLRVELLGETSIAECLTYLDNG VVFVGSRLGDSQLVKLNVDSNEQGSYVVAMETFTNLGPIV DMCVVDLERQGQGQLVTCSGAFKEGSLRIIRNGKLHIRTV PLYESPRKICYQEVSQCFGVLSSRIEVQDTSGGTTALRPS ASTQALSSSVSSSKLFSSSTAPHETSFGEEVEVHNLLIID QHTFEVLHAHQFLQNEYALSLVSCKLGKDPNTYFIVGTAM VYPEEAEPKQGRIVVFQYSDGKLQTVAEKEVKGAVYSMVE FNGKLLASINSTVRLYEWTTEKELRTECNHYNNIMALYLK TKGDFILVGDLMRSVLLLAYKPMEGNFEEIARDFNPNWMS AVEILDDDNFLGAENAFNLFVCQKDSAATTDEERQHLQEV GLFHLGEFVNVFCHGSLVMQNLGETSTPTQGSVLFGTVNG MIGLVTSLSESWYNLLLDMQNRLNKVIKSVGKIEHSFWRS FHTERKTEPATGFIDGDLIESFLDISRPKMQEVVANLQYD DGSGMKREATADDLIKVVEELTRIH L:  QILPPCRSIVRTLHQHKLGRASWPSVQQGLQQSFLHTLDS YRILQKAAPFDRRATSLAWHPTHPSTVAVGSKGGDIMLWN FGIKDKPTFIKGIGAGGSITGLKFNPLNTNQFYASSMEGT TRLQDFKGNILRVFASSDTINIWFCSLDVSASSRMVVTGD NVGNVILLNMDGKELWNLRMHKKKVTHVALNPCCDWFLAT ASVDQTVKIWDLRQVRGKASFLYSLPHRHPVNAACFSPDG ARLLTTDQKSEIRVYSASQWDCPLGLIPHPHRHFQHLTPI KAAWHPRYNLIVVGRYPDPNFKSCTPYELRTIDVFDGNSG KMMCQLYDPESSGISSLNEFNPMGDTLASAMGYHILIWSQ EEARTRK 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 1, DNA damage-binding protein 2/DNA Complex Functional site 1) chain D residue 37 type MOD_RES sequence S description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 2) chain H residue 37 type MOD_RES sequence S description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 3) chain E residue 57 type MOD_RES sequence K description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 4) chain D residue 47 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 5) chain D residue 109 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 6) chain H residue 47 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 7) chain H residue 109 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 8) chain D residue 80 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 9) chain H residue 80 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 10) chain D residue 113 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 11) chain H residue 113 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 12) chain B residue 80 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 13) chain F residue 60 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 14) chain F residue 80 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 15) chain D residue 58 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI12 16) chain H residue 58 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI12 17) chain G residue 120 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine; alternate => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI12 18) 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 19) 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 20) 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 21) 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 22) 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 23) chain B residue 45 type MOD_RES sequence K description N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322 source Swiss-Prot : SWS_FT_FI5 24) chain F residue 45 type MOD_RES sequence K description N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322 source Swiss-Prot : SWS_FT_FI5 25) chain B residue 78 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 26) chain B residue 92 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 27) chain F residue 32 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 28) chain F residue 78 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 29) chain F residue 92 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 30) chain G residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI7 31) chain G residue 76 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI7 32) chain D residue 35 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 33) chain D residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 34) chain D residue 121 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 35) chain H residue 35 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 36) chain H residue 117 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 37) chain H residue 121 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 38) chain D residue 36 type MOD_RES sequence E description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 39) chain H residue 36 type MOD_RES sequence E description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 40) chain G residue 119 type MOD_RES sequence K description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 41) chain G residue 120 type MOD_RES sequence K description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 42) chain L residue 258-272 type prosite sequence LATASVDQTVKIWDL description WD_REPEATS_1 Trp-Asp (WD) repeats signature. LATAsvDqTVKIWDL source prosite : PS00678 43) chain D residue 93-115 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 44) chain A residue 67-75 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 45) chain C residue 22-28 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 46) 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 47) 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 48) chain A residue 81 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI22 49) chain E residue 81 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI22 50) chain A residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI23 51) chain E residue 87 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI23 52) chain A residue 108 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI24 53) chain E residue 108 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI24 54) chain A residue 116 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI25 55) chain E residue 116 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI25 56) 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 57) 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 58) 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 59) 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 60) 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 61) chain D residue 87 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 62) chain D residue 93 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 63) chain H residue 87 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 64) chain H residue 93 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 65) chain D residue 116 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 66) chain H residue 116 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 67) chain F residue 92 type MOD_RES sequence K description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 68) chain H residue 44 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:32789493 source Swiss-Prot : SWS_FT_FI3 69) chain H residue 86 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:32789493 source Swiss-Prot : SWS_FT_FI3 70) chain L residue 77 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:32789493 source Swiss-Prot : SWS_FT_FI3 71) chain D residue 44 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:32789493 source Swiss-Prot : SWS_FT_FI3 72) chain D residue 86 type MOD_RES sequence K description N6-acetyllysine => ECO:0000269|PubMed:32789493 source Swiss-Prot : SWS_FT_FI3

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