eF-site ID 2g6q-A PDB Code 2g6q Chain A click to enlarge Title Crystal structure of ING2 PHD finger in complex with H3K4Me3 peptide Classification GENE REGULATION, APOPTOSIS Compound Inhibitor of growth protein 2 Source Mus musculus (Mouse) (2G6Q) Sequence A:  EPTYCLCNQVSYGEMIGCDNEQCPIEWFHFSCVSLTYKPK GKWYCPKCRGDN Description Functional site 1) chain A residue 216 type sequence C description BINDING SITE FOR RESIDUE ZN A 300 source : AC1 2) chain A residue 218 type sequence C description BINDING SITE FOR RESIDUE ZN A 300 source : AC1 3) chain A residue 240 type sequence H description BINDING SITE FOR RESIDUE ZN A 300 source : AC1 4) chain A residue 243 type sequence C description BINDING SITE FOR RESIDUE ZN A 300 source : AC1 5) chain A residue 229 type sequence C description BINDING SITE FOR RESIDUE ZN A 400 source : AC2 6) chain A residue 234 type sequence C description BINDING SITE FOR RESIDUE ZN A 400 source : AC2 7) chain A residue 256 type sequence C description BINDING SITE FOR RESIDUE ZN A 400 source : AC2 8) chain A residue 259 type sequence C description BINDING SITE FOR RESIDUE ZN A 400 source : AC2 9) chain A residue 213-262 type ZN_FING sequence PTYCLCNQVSYGEMIGCDNEQCPIEWFHFSCVSLTYKPKG KWYCPKCRGD description PHD-type => ECO:0000255|PROSITE-ProRule:PRU00146 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 216-259 type prosite sequence CLCNQVSYGEMIGCDNEQCPIEWFHFSCVSLTYKPKGKWY CPKC description ZF_PHD_1 Zinc finger PHD-type signature. Cl.Cnqvsygem.....................................IgCdneqCpiewFHfsCvsltykpkgk...................................WyCpkC source prosite : PS01359 11) chain A residue 216 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI2 12) chain A residue 218 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 229 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 234 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 240 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 243 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 256 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 259 type BINDING sequence C description BINDING => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 215 type SITE sequence Y description Histone H3K4me3 binding => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI3 20) chain A residue 226 type SITE sequence M description Histone H3K4me3 binding => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI3 21) chain A residue 230 type SITE sequence D description Histone H3K4me3 binding => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI3 22) chain A residue 238 type SITE sequence W description Histone H3K4me3 binding => ECO:0000250|UniProtKB:Q9UK53 source Swiss-Prot : SWS_FT_FI3

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