eF-site ID 3azm-ABCDEFGH PDB Code 3azm Chain A, B, C, D, E, F, G, H click to enlarge Title Crystal Structure of Human Nucleosome Core Particle Containing H4K79Q mutation Classification STRUCTURAL PROTEIN/DNA Compound Histone H3.1 Source null (3AZM) Sequence A:  PHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQD FKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRV TIMPKDIQLARRIRGERA B:  NIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLEN VIRDAVTYTEHAKRQTVTAMDVVYALKRQGRTLYGFG C:  KAKTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLA AVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEE LNKLLGRVTIAQGGVLPNIQAVLLPK D:  KRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDI FERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKH AVSEGTKAVTKYTSA E:  KPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQ DFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKR VTIMPKDIQLARRIRGERA F:  RKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVL KVFLENVIRDAVTYTEHAKRQTVTAMDVVYALKRQGRTLY GFGG G:  KTRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAV LEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELN KLLGRVTIAQGGVLPNIQAVLLPK H:  RKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFER IAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVS EGTKAVTKYTSA Description Functional site 1) chain A residue 121 type sequence P description BINDING SITE FOR RESIDUE CL A 1001 source : AC1 2) chain A residue 122 type sequence K description BINDING SITE FOR RESIDUE CL A 1001 source : AC1 3) chain C residue 44 type sequence G description BINDING SITE FOR RESIDUE CL C 1001 source : AC2 4) chain C residue 45 type sequence A description BINDING SITE FOR RESIDUE CL C 1001 source : AC2 5) chain C residue 46 type sequence G description BINDING SITE FOR RESIDUE CL C 1001 source : AC2 6) chain C residue 47 type sequence A description BINDING SITE FOR RESIDUE CL C 1001 source : AC2 7) chain D residue 91 type sequence S description BINDING SITE FOR RESIDUE CL C 1001 source : AC2 8) chain D residue 48 type sequence V description BINDING SITE FOR RESIDUE MN E 1001 source : AC3 9) chain E residue 77 type sequence D description BINDING SITE FOR RESIDUE MN E 1001 source : AC3 10) chain G residue 44 type sequence G description BINDING SITE FOR RESIDUE CL G 1001 source : AC4 11) chain G residue 45 type sequence A description BINDING SITE FOR RESIDUE CL G 1001 source : AC4 12) chain G residue 46 type sequence G description BINDING SITE FOR RESIDUE CL G 1001 source : AC4 13) chain G residue 47 type sequence A description BINDING SITE FOR RESIDUE CL G 1001 source : AC4 14) chain D residue 112 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 15) chain H residue 112 type CARBOHYD sequence S description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 16) chain B residue 79 type CARBOHYD sequence Q description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 17) chain F residue 20 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 18) chain F residue 59 type CARBOHYD sequence K description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 19) chain F residue 79 type CARBOHYD sequence Q description O-linked (GlcNAc) serine => ECO:0000250|UniProtKB:P62807 source Swiss-Prot : SWS_FT_FI16 20) 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 21) 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 22) chain A residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711 source Swiss-Prot : SWS_FT_FI21 23) chain E residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:29211711 source Swiss-Prot : SWS_FT_FI21 24) chain A residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI22 25) chain E residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:20850016 source Swiss-Prot : SWS_FT_FI22 26) chain A residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI23 27) chain E residue 86 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P84243 source Swiss-Prot : SWS_FT_FI23 28) chain A residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI24 29) chain E residue 107 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q71DI3 source Swiss-Prot : SWS_FT_FI24 30) chain A residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI25 31) chain E residue 115 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI25 32) chain A residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229 source Swiss-Prot : SWS_FT_FI26 33) chain E residue 122 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435, ECO:0000269|PubMed:27436229 source Swiss-Prot : SWS_FT_FI26 34) 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 35) 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 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 F residue 77 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 39) chain F residue 91 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 40) chain B residue 77 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 41) chain B residue 91 type MOD_RES sequence K description Phosphoserine; by STK4/MST1 => ECO:0000269|PubMed:12757711 source Swiss-Prot : SWS_FT_FI6 42) chain F residue 31 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 34 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 48) chain D residue 116 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 49) chain D residue 120 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 50) chain H residue 34 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI8 51) chain G residue 118 type MOD_RES sequence K description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 52) chain D residue 35 type MOD_RES sequence E description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 53) chain H residue 35 type MOD_RES sequence E description PolyADP-ribosyl glutamic acid => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI9 54) chain H residue 43 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 55) chain H residue 85 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 56) chain D residue 43 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 57) chain D residue 85 type MOD_RES sequence K description N6-lactoyllysine; alternate => ECO:0000269|PubMed:31645732 source Swiss-Prot : SWS_FT_FI3 58) chain G residue 95 type MOD_RES sequence K description ADP-ribosylserine => ECO:0000269|PubMed:34874266 source Swiss-Prot : SWS_FT_FI4 59) chain E residue 56 type MOD_RES sequence K description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 60) chain D residue 36 type MOD_RES sequence S description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 61) chain H residue 36 type MOD_RES sequence S description Phosphoserine; by AMPK => ECO:0000250|UniProtKB:Q64475 source Swiss-Prot : SWS_FT_FI10 62) chain D residue 46 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 63) chain D residue 108 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 64) chain H residue 46 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 65) chain H residue 108 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:16627869 source Swiss-Prot : SWS_FT_FI11 66) 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 67) 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 68) chain D residue 79 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 69) chain H residue 79 type MOD_RES sequence R description Dimethylated arginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI13 70) chain H residue 86 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 71) chain H residue 92 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 72) chain D residue 86 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 73) chain D residue 92 type MOD_RES sequence R description Omega-N-methylarginine => ECO:0000250|UniProtKB:Q96A08 source Swiss-Prot : SWS_FT_FI14 74) chain D residue 115 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 75) chain H residue 115 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 76) chain F residue 91 type MOD_RES sequence K description Phosphothreonine => ECO:0000250|UniProtKB:Q00729 source Swiss-Prot : SWS_FT_FI15 77) chain D residue 92-114 type prosite sequence REIQTAVRLLLPGELAKHAVSEG description HISTONE_H2B Histone H2B signature. REIQTavRlLLpGELaKHAVSEG source prosite : PS00357 78) chain A residue 66-74 type prosite sequence PFQRLVREI description HISTONE_H3_2 Histone H3 signature 2. PFqRLVREI source prosite : PS00959 79) chain C residue 21-27 type prosite sequence AGLQFPV description HISTONE_H2A Histone H2A signature. AGLqFPV source prosite : PS00046

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