eF-site ID 2jmj_11-AP PDB Code 2jmj Model 11 Chain A, P click to enlarge Title NMR solution structure of the PHD domain from the yeast YNG1 protein in complex with H3(1-9)K4me3 peptide Classification PROTEIN BINDING Compound Protein YNG1 Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (H3_YEAST) Sequence A:  QEEVYCFCRNVSYGPMVACDNPACPFEWFHYGCVGLKQAP KGKWYCSKDCKEIANQRSKS P:  ARTXQTARK Description Functional site 1) chain A residue 42 type sequence C description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 2) chain A residue 47 type sequence C description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 3) chain A residue 52 type sequence F description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 4) chain A residue 69 type sequence C description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 5) chain A residue 73 type sequence C description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 6) chain A residue 29 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 7) chain A residue 31 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 8) chain A residue 33 type sequence N description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 9) chain A residue 36 type sequence Y description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 10) chain A residue 53 type sequence H description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 11) chain A residue 56 type sequence C description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 12) chain P residue 4 type MOD_RES sequence X description N6-methyllysine; alternate => ECO:0000269|PubMed:11742990, ECO:0000269|PubMed:11751634, ECO:0000269|PubMed:11752412, ECO:0000269|PubMed:12152067, ECO:0000269|PubMed:12353038, ECO:0000269|PubMed:12845608, ECO:0000269|PubMed:15949446, ECO:0000269|PubMed:16122352, ECO:0000269|PubMed:16168379, ECO:0000269|PubMed:16185711, ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI1 13) chain P residue 9 type MOD_RES sequence K description N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 31 type MOD_RES sequence C description N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 42 type MOD_RES sequence C description N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 47 type MOD_RES sequence C description N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 53 type MOD_RES sequence H description N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 56 type MOD_RES sequence C description N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 69 type MOD_RES sequence C description N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 73 type MOD_RES sequence C description N6-methyllysine; alternate => ECO:0000269|PubMed:17194708 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 28 type SITE sequence Y description Histone H3K4me3 binding => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 39 type SITE sequence M description Histone H3K4me3 binding => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI3 23) chain A residue 43 type SITE sequence D description Histone H3K4me3 binding => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI3 24) chain A residue 51 type SITE sequence W description Histone H3K4me3 binding => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI3

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