eF-site ID 3c6w-ABCD PDB Code 3c6w Chain A, B, C, D click to enlarge Title Crystal structure of the ING5 PHD finger in complex with H3K4me3 peptide Classification METAL BINDING PROTEIN Compound Inhibitor of growth protein 5 Source Homo sapiens (Human) (3C6W) Sequence A:  EPTYCLCHQVSYGEMIGCDNPDCPIEWFHFACVDLTTKPK GKWFCPRCVQE B:  ARTXQTA C:  NEPTYCLCHQVSYGEMIGCDNPDCPIEWFHFACVDLTTKP KGKWFCPRCVQE D:  ARTXQTARKST Description (1)  Inhibitor of growth protein 5 Functional site 1) chain A residue 189 type sequence C description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 2) chain A residue 191 type sequence C description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 3) chain A residue 213 type sequence H description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 4) chain A residue 216 type sequence C description BINDING SITE FOR RESIDUE ZN A 1 source : AC1 5) chain A residue 202 type sequence C description BINDING SITE FOR RESIDUE ZN A 2 source : AC2 6) chain A residue 207 type sequence C description BINDING SITE FOR RESIDUE ZN A 2 source : AC2 7) chain A residue 229 type sequence C description BINDING SITE FOR RESIDUE ZN A 2 source : AC2 8) chain A residue 232 type sequence C description BINDING SITE FOR RESIDUE ZN A 2 source : AC2 9) chain C residue 189 type sequence C description BINDING SITE FOR RESIDUE ZN C 3 source : AC3 10) chain C residue 191 type sequence C description BINDING SITE FOR RESIDUE ZN C 3 source : AC3 11) chain C residue 213 type sequence H description BINDING SITE FOR RESIDUE ZN C 3 source : AC3 12) chain C residue 216 type sequence C description BINDING SITE FOR RESIDUE ZN C 3 source : AC3 13) chain C residue 202 type sequence C description BINDING SITE FOR RESIDUE ZN C 4 source : AC4 14) chain C residue 207 type sequence C description BINDING SITE FOR RESIDUE ZN C 4 source : AC4 15) chain C residue 229 type sequence C description BINDING SITE FOR RESIDUE ZN C 4 source : AC4 16) chain C residue 232 type sequence C description BINDING SITE FOR RESIDUE ZN C 4 source : AC4 17) chain A residue 186-235 type ZN_FING sequence PTYCLCHQVSYGEMIGCDNPDCPIEWFHFACVDLTTKPKG KWFCPRCVQE description PHD-type => ECO:0000255|PROSITE-ProRule:PRU00146 source Swiss-Prot : SWS_FT_FI1 18) chain C residue 186-235 type ZN_FING sequence PTYCLCHQVSYGEMIGCDNPDCPIEWFHFACVDLTTKPKG KWFCPRCVQE description PHD-type => ECO:0000255|PROSITE-ProRule:PRU00146 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 189 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 20) chain A residue 191 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 21) chain A residue 202 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 22) chain C residue 191 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 23) chain C residue 202 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 24) chain C residue 207 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 25) chain C residue 213 type BINDING sequence H description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 26) chain C residue 216 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 27) chain C residue 229 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 28) chain C residue 232 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 29) chain A residue 229 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 30) chain A residue 232 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 31) chain C residue 189 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 32) chain A residue 207 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 33) chain A residue 213 type BINDING sequence H description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 34) chain A residue 216 type BINDING sequence C description BINDING => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI2 35) chain A residue 188 type SITE sequence Y description Histone H3K4me3 binding => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI3 36) chain A residue 199 type SITE sequence M description Histone H3K4me3 binding => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI3 37) chain A residue 203 type SITE sequence D description Histone H3K4me3 binding => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI3 38) chain A residue 211 type SITE sequence W description Histone H3K4me3 binding => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI3 39) chain C residue 188 type SITE sequence Y description Histone H3K4me3 binding => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI3 40) chain C residue 199 type SITE sequence M description Histone H3K4me3 binding => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI3 41) chain C residue 203 type SITE sequence D description Histone H3K4me3 binding => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI3 42) chain C residue 211 type SITE sequence W description Histone H3K4me3 binding => ECO:0000269|PubMed:18623064, ECO:0007744|PDB:3C6W source Swiss-Prot : SWS_FT_FI3 43) chain A residue 189-232 type prosite sequence CLCHQVSYGEMIGCDNPDCPIEWFHFACVDLTTKPKGKWF CPRC description ZF_PHD_1 Zinc finger PHD-type signature. Cl.Chqvsygem.....................................IgCdnpdCpiewFHfaCvdlttkpkgk...................................WfCprC source prosite : PS01359

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