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4YAD

Crystal structure of TRIM24 PHD-bromodomain complexed with 2,4-dimethoxy-N-(1-methyl-2-oxo-1,2,3,4-tetrahydroquinolin-6-yl)benzene-1-sulfonamide (3b)

Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 1101
ChainResidue
ACYS829
ACYS832
AHIS849
ACYS852

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN A 1102
ChainResidue
ACYS841
ACYS844
ACYS867
ACYS870

site_idAC3
Number of Residues10
Detailsbinding site for residue 4A7 A 1103
ChainResidue
APHE924
APRO929
AVAL932
AASN980
AGLU985
AHOH1258
AHOH1259
AHOH1283
AHOH1302
AALA923

site_idAC4
Number of Residues7
Detailsbinding site for residue GOL A 1104
ChainResidue
ASER851
ATHR856
ALYS949
AHOH1208
AHOH1320
AHOH1342
AHOH1366

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 1101
ChainResidue
BCYS829
BCYS832
BHIS849
BCYS852

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN B 1102
ChainResidue
BCYS841
BCYS844
BCYS867
BCYS870

site_idAC7
Number of Residues8
Detailsbinding site for residue 4A7 B 1103
ChainResidue
BALA923
BPHE924
BVAL928
BPRO929
BPHE979
BASN980
BHOH1219
BHOH1249

site_idAC8
Number of Residues4
Detailsbinding site for residue GOL B 1104
ChainResidue
BARG910
BASN1003
BLEU1004
BHOH1226

site_idAC9
Number of Residues1
Detailsbinding site for residue CL B 1105
ChainResidue
BARG906

Functional Information from PROSITE/UniProt
site_idPS00633
Number of Residues62
DetailsBROMODOMAIN_1 Bromodomain signature. HemSlafqDpvpltvpDYYkiIknpMdlstIkkrlqedysmYskpedfvadfrl.IfqNCaeF
ChainResidueDetails
AHIS918-PHE979

site_idPS01359
Number of Residues42
DetailsZF_PHD_1 Zinc finger PHD-type signature. CavCqnggel.......................................LcCek..Cpkv.FHlsChvptltnfpsge.................................WiCtfC
ChainResidueDetails
ACYS829-CYS870

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues210
DetailsDomain: {"description":"Bromo","evidences":[{"source":"PROSITE-ProRule","id":"PRU00035","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues94
DetailsZinc finger: {"description":"PHD-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00146","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues12
DetailsRegion: {"description":"Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsRegion: {"description":"Interaction with histone H3 that is acetylated at 'Lys-23' (H3K23ac)"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues32
DetailsMotif: {"description":"Nuclear localization signal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsSite: {"description":"Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"PubMed","id":"25218447","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

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