eF-site ID 2qic-AB PDB Code 2qic Chain A, B click to enlarge Title Crystal Structure of the ING1 PHD Finger in complex with a Histone H3K4ME3 peptide Classification ANTITUMOR PROTEIN, APOPTOSIS Compound Inhibitor of growth protein 1 Source Homo sapiens (Human) (2QIC) Sequence A:  EPTYCLCNQVSYGEMIGCDNDECPIEWFHFSCVGLNHKPK GKWYCPKCRGE B:  ARTXQTAR Description Functional site 1) chain A residue 213 type sequence C description BINDING SITE FOR RESIDUE ZN A 300 source : AC1 2) chain A residue 215 type sequence C description BINDING SITE FOR RESIDUE ZN A 300 source : AC1 3) chain A residue 237 type sequence H description BINDING SITE FOR RESIDUE ZN A 300 source : AC1 4) chain A residue 240 type sequence C description BINDING SITE FOR RESIDUE ZN A 300 source : AC1 5) chain A residue 226 type sequence C description BINDING SITE FOR RESIDUE ZN A 400 source : AC2 6) chain A residue 231 type sequence C description BINDING SITE FOR RESIDUE ZN A 400 source : AC2 7) chain A residue 253 type sequence C description BINDING SITE FOR RESIDUE ZN A 400 source : AC2 8) chain A residue 256 type sequence C description BINDING SITE FOR RESIDUE ZN A 400 source : AC2 9) chain A residue 210-259 type ZN_FING sequence PTYCLCNQVSYGEMIGCDNDECPIEWFHFSCVGLNHKPKG KWYCPKCRGE description PHD-type => ECO:0000255|PROSITE-ProRule:PRU00146 source Swiss-Prot : SWS_FT_FI1 10) chain A residue 213 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC source Swiss-Prot : SWS_FT_FI2 11) chain A residue 215 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC source Swiss-Prot : SWS_FT_FI2 12) chain A residue 226 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC source Swiss-Prot : SWS_FT_FI2 13) chain A residue 231 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC source Swiss-Prot : SWS_FT_FI2 14) chain A residue 237 type BINDING sequence H description BINDING => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC source Swiss-Prot : SWS_FT_FI2 15) chain A residue 240 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC source Swiss-Prot : SWS_FT_FI2 16) chain A residue 253 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC source Swiss-Prot : SWS_FT_FI2 17) chain A residue 256 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC source Swiss-Prot : SWS_FT_FI2 18) chain A residue 212 type SITE sequence Y description Histone H3K4me3 binding => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC source Swiss-Prot : SWS_FT_FI3 19) chain A residue 223 type SITE sequence M description Histone H3K4me3 binding => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC source Swiss-Prot : SWS_FT_FI3 20) chain A residue 227 type SITE sequence D description Histone H3K4me3 binding => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC source Swiss-Prot : SWS_FT_FI3 21) chain A residue 235 type SITE sequence W description Histone H3K4me3 binding => ECO:0000269|PubMed:18533182, ECO:0007744|PDB:2QIC source Swiss-Prot : SWS_FT_FI3 22) chain A residue 213-256 type prosite sequence CLCNQVSYGEMIGCDNDECPIEWFHFSCVGLNHKPKGKWY CPKC description ZF_PHD_1 Zinc finger PHD-type signature. Cl.Cnqvsygem.....................................IgCdndeCpiewFHfsCvglnhkpkgk...................................WyCpkC source prosite : PS01359

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