eF-site ID 3r45-ABC PDB Code 3r45 Chain A, B, C click to enlarge Title Structure of a CENP-A-Histone H4 Heterodimer in complex with chaperone HJURP Classification NUCLEAR PROTEIN Compound Histone H3-like centromeric protein A Source Homo sapiens (Human) (HJURP_HUMAN) Sequence A:  HLLIRKLPFSRLAREICVKFTRGVDFNWQAQALLALQEAA EAFLVHLFEDAYLLTLHAGRVTLFPKDVQLARRIRGLEEG LG B:  RDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFL ENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRT C:  EDDQLLQKLRASRRRFQRRMQRLIEKYNQPFEDTPVVQMA TLTYETPQGLRIWGGRLIKER Description Functional site 1) chain A residue 63 type sequence R description BINDING SITE FOR RESIDUE SO4 A 141 source : AC1 2) chain A residue 64 type sequence K description BINDING SITE FOR RESIDUE SO4 A 141 source : AC1 3) chain C residue 67 type sequence G description BINDING SITE FOR RESIDUE SO4 A 141 source : AC1 4) chain A residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 A 142 source : AC2 5) chain A residue 72 type sequence R description BINDING SITE FOR RESIDUE SO4 A 142 source : AC2 6) chain C residue 72 type sequence K description BINDING SITE FOR RESIDUE SO4 A 142 source : AC2 7) chain C residue 74 type sequence R description BINDING SITE FOR RESIDUE SO4 A 142 source : AC2 8) chain A residue 118 type sequence R description BINDING SITE FOR RESIDUE SO4 A 143 source : AC3 9) chain A residue 124 type sequence K description BINDING SITE FOR RESIDUE SO4 A 143 source : AC3 10) chain A residue 118 type sequence R description BINDING SITE FOR RESIDUE SO4 A 144 source : AC4 11) chain A residue 118 type sequence R description BINDING SITE FOR RESIDUE SO4 A 144 source : AC4 12) chain A residue 119 type sequence V description BINDING SITE FOR RESIDUE SO4 A 144 source : AC4 13) chain A residue 119 type sequence V description BINDING SITE FOR RESIDUE SO4 A 144 source : AC4 14) chain A residue 120 type sequence T description BINDING SITE FOR RESIDUE SO4 A 144 source : AC4 15) chain A residue 120 type sequence T description BINDING SITE FOR RESIDUE SO4 A 144 source : AC4 16) chain A residue 63 type sequence R description BINDING SITE FOR RESIDUE SO4 B 103 source : AC6 17) chain B residue 30 type sequence T description BINDING SITE FOR RESIDUE SO4 B 103 source : AC6 18) chain B residue 32 type sequence P description BINDING SITE FOR RESIDUE SO4 B 103 source : AC6 19) chain B residue 36 type sequence R description BINDING SITE FOR RESIDUE SO4 B 103 source : AC6 20) chain B residue 77 type sequence K description BINDING SITE FOR RESIDUE SO4 B 104 source : AC7 21) chain B residue 78 type sequence R description BINDING SITE FOR RESIDUE SO4 B 104 source : AC7 22) chain B residue 79 type sequence K description BINDING SITE FOR RESIDUE SO4 B 104 source : AC7 23) chain B residue 80 type sequence T description BINDING SITE FOR RESIDUE SO4 B 104 source : AC7 24) chain B residue 31 type sequence K description BINDING SITE FOR RESIDUE SO4 B 105 source : AC8 25) chain B residue 35 type sequence R description BINDING SITE FOR RESIDUE SO4 B 105 source : AC8 26) chain B residue 30 type sequence T description BINDING SITE FOR RESIDUE SO4 B 106 source : AC9 27) chain B residue 31 type sequence K description BINDING SITE FOR RESIDUE SO4 B 106 source : AC9 28) chain B residue 32 type sequence P description BINDING SITE FOR RESIDUE SO4 B 106 source : AC9 29) chain B residue 55 type sequence R description BINDING SITE FOR RESIDUE SO4 B 106 source : AC9 30) chain B residue 39 type sequence R description BINDING SITE FOR RESIDUE GOL B 107 source : BC1 31) chain B residue 45 type sequence R description BINDING SITE FOR RESIDUE GOL B 107 source : BC1 32) chain C residue 23 type sequence R description BINDING SITE FOR RESIDUE SO4 C 81 source : BC2 33) chain C residue 27 type sequence R description BINDING SITE FOR RESIDUE SO4 C 81 source : BC2 34) chain C residue 31 type sequence R description BINDING SITE FOR RESIDUE SO4 C 81 source : BC2 35) chain C residue 35 type sequence R description BINDING SITE FOR RESIDUE SO4 C 81 source : BC2 36) chain B residue 71 type sequence T description BINDING SITE FOR RESIDUE SO4 C 82 source : BC3 37) chain C residue 42 type sequence Q description BINDING SITE FOR RESIDUE SO4 C 82 source : BC3 38) chain C residue 43 type sequence P description BINDING SITE FOR RESIDUE SO4 C 82 source : BC3 39) chain C residue 44 type sequence F description BINDING SITE FOR RESIDUE SO4 C 82 source : BC3 40) chain C residue 45 type sequence E description BINDING SITE FOR RESIDUE SO4 C 82 source : BC3 41) chain C residue 64 type sequence R description BINDING SITE FOR RESIDUE SO4 C 83 source : BC4 42) chain C residue 69 type sequence R description BINDING SITE FOR RESIDUE SO4 C 83 source : BC4 43) chain C residue 70 type sequence L description BINDING SITE FOR RESIDUE SO4 C 83 source : BC4 44) chain C residue 15 type sequence D description BINDING SITE FOR RESIDUE SO4 C 84 source : BC5 45) chain A residue 87 type sequence Q description BINDING SITE FOR RESIDUE SO4 C 85 source : BC6 46) chain B residue 77 type sequence K description BINDING SITE FOR RESIDUE SO4 C 85 source : BC6 47) chain C residue 45 type sequence E description BINDING SITE FOR RESIDUE SO4 C 85 source : BC6 48) chain C residue 24 type sequence A description BINDING SITE FOR RESIDUE GOL C 86 source : BC7 49) chain C residue 27 type sequence R description BINDING SITE FOR RESIDUE GOL C 86 source : BC7 50) chain C residue 28 type sequence R description BINDING SITE FOR RESIDUE GOL C 86 source : BC7 51) chain C residue 31 type sequence R description BINDING SITE FOR RESIDUE GOL C 86 source : BC7 52) chain C residue 35 type sequence R description BINDING SITE FOR RESIDUE GOL C 86 source : BC7 53) chain A residue 66-74 type prosite sequence PFSRLAREI description HISTONE_H3_2 Histone H3 signature 2. PFsRLAREI source prosite : PS00959 54) chain B residue 59 type MOD_RES sequence K description N6-glutaryllysine; alternate => ECO:0000269|PubMed:31542297 source Swiss-Prot : SWS_FT_FI10 55) chain B residue 79 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P62806 source Swiss-Prot : SWS_FT_FI11 56) chain B residue 80 type MOD_RES sequence T description Phosphothreonine => ECO:0000250|UniProtKB:P62806 source Swiss-Prot : SWS_FT_FI12 57) chain B residue 88 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:24275569 source Swiss-Prot : SWS_FT_FI13 58) chain B residue 91 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 59) chain B residue 59 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 60) chain B residue 79 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 61) chain B residue 31 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 62) chain B residue 44 type MOD_RES sequence K description N6-propionyllysine; alternate => ECO:0000269|PubMed:17267393 source Swiss-Prot : SWS_FT_FI5 63) chain B residue 31 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI6 64) chain B residue 77 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI6 65) chain B residue 91 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000269|PubMed:22389435 source Swiss-Prot : SWS_FT_FI6 66) chain B residue 47 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 67) chain B residue 51 type MOD_RES sequence Y description Phosphotyrosine => ECO:0007744|PubMed:15592455, ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI9

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