eF-site ID 5zbx-ABCDEFGH PDB Code 5zbx Chain A, B, C, D, E, F, G, H click to enlarge Title The crystal structure of the nucleosome containing histone H3.1 CATD(V76Q, K77D) Classification DNA BINDING PROTEIN/DNA Compound Histone H3.1,Histone H3-like centromeric protein A,Histone H3.1 Source (5ZBX) Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREICQD FTDFNWQAQALLALQEAAEAFLVHLFEDAYLLTLHAKRVT IMPKDIQLARRIRGE B:  NIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLEN VIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFG C:  RAKAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVY LAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRND EELNKLLGRVTIAQGGVLPNIQAVLLPK D:  SRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFE RIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAV SEGTKAVTKYTSA E:  VKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREI CQDFTRGVDFNWQAQALLALQEAAEAFLVHLFEDAYLLTL HAKRVTIMPKDIQLARRIRGE F:  HRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGV LKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTL YGFGG G:  KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAV LEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELN KLLGRVTIAQGGVLPNIQAVLLPK H:  RKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFER IAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVS EGTKAVTKYTSA Description Functional site 1) chain C residue 46 type sequence G description binding site for residue CL C 201 source : AC1 2) chain C residue 47 type sequence A description binding site for residue CL C 201 source : AC1 3) chain D residue 90 type sequence T description binding site for residue CL C 201 source : AC1 4) chain D residue 91 type sequence S description binding site for residue CL C 201 source : AC1 5) chain D residue 48 type sequence V description binding site for residue MN E 1001 source : AC2 6) chain E residue 77 type sequence D description binding site for residue MN E 1001 source : AC2 7) chain G residue 46 type sequence G description binding site for residue CL G 2001 source : AC3 8) chain G residue 47 type sequence A description binding site for residue CL G 2001 source : AC3 9) chain H residue 90 type sequence T description binding site for residue CL G 2001 source : AC3 10) chain H residue 91 type sequence S description binding site for residue CL G 2001 source : AC3 11) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 12) 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 13) 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 14) 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 15) 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 16) chain H residue 35 type MOD_RES sequence E description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 17) chain D residue 35 type MOD_RES sequence E description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 18) chain G residue 118 type MOD_RES sequence K description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 19) chain B residue 79 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 20) chain F residue 20 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 21) chain F residue 59 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 22) chain F residue 79 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 23) chain D residue 112 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 24) chain H residue 112 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 25) chain A residue 117 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI21 26) chain E residue 117 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI21 27) chain A residue 124 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229 source Swiss-Prot : SWS_FT_FI22 28) chain E residue 124 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229 source Swiss-Prot : SWS_FT_FI22 29) chain D residue 92-114 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 30) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046 31) chain H residue 43 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 32) chain H residue 85 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 33) chain D residue 43 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 34) chain D residue 85 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 35) chain G residue 95 type MOD_RES sequence K description ADP-ribosylserine => ECO:0000269|PubMed:34874266 source Swiss-Prot : SWS_FT_FI4 36) chain B residue 44 type MOD_RES sequence K description N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322 source Swiss-Prot : SWS_FT_FI5 37) chain F residue 44 type MOD_RES sequence K description N6-crotonyllysine; alternate => ECO:0000269|PubMed:21925322 source Swiss-Prot : SWS_FT_FI5 38) chain B residue 77 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 39) chain B residue 91 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 40) chain F residue 31 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 41) chain F residue 77 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 42) chain F residue 91 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 43) chain G residue 74 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI7 44) chain G residue 75 type MOD_RES sequence K description N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:24681537 source Swiss-Prot : SWS_FT_FI7 45) chain H residue 116 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 46) chain H residue 120 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 47) chain D residue 116 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 48) chain D residue 120 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 49) chain H residue 34 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 50) chain D residue 34 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 51) chain E residue 56 type MOD_RES sequence K description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 52) chain D residue 36 type MOD_RES sequence S description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 53) chain H residue 36 type MOD_RES sequence S description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 54) chain H residue 46 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 55) chain H residue 108 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 56) chain D residue 46 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 57) chain D residue 108 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 58) 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 59) 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 60) chain D residue 79 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 61) chain H residue 79 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 62) chain H residue 86 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 63) chain H residue 92 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 64) chain D residue 86 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 65) chain D residue 92 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 66) chain F residue 91 type MOD_RES sequence K description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 67) chain D residue 115 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 68) chain H residue 115 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15

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