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5H1T

Complex structure of TRIM24 PHD-bromodomain and inhibitor 1

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 Residues7
Detailsbinding site for residue 7FF A 1103
ChainResidue
APHE924
APRO929
APHE979
AASN980
AVAL986
AHOH1208
AALA923

site_idAC4
Number of Residues5
Detailsbinding site for residue DMS A 1104
ChainResidue
ALYS846
APHE914
ATYR956
ATYR996
AHOH1215

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 Residues4
Detailsbinding site for residue 7FF B 1103
ChainResidue
BALA923
BPHE924
BASN980
BHOH1203

site_idAC8
Number of Residues2
Detailsbinding site for residue DMS B 1104
ChainResidue
BPRO902
BARG906

site_idAC9
Number of Residues4
Detailsbinding site for residue ZN C 1101
ChainResidue
CCYS841
CCYS844
CCYS867
CCYS870

site_idAD1
Number of Residues4
Detailsbinding site for residue ZN C 1102
ChainResidue
CCYS829
CCYS832
CHIS849
CCYS852

site_idAD2
Number of Residues5
Detailsbinding site for residue 7FF C 1103
ChainResidue
CALA923
CPHE924
CPRO929
CASN980
CHOH1207

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN D 1101
ChainResidue
DCYS829
DCYS832
DHIS849
DCYS852

site_idAD4
Number of Residues4
Detailsbinding site for residue ZN D 1102
ChainResidue
DCYS841
DCYS844
DCYS867
DCYS870

site_idAD5
Number of Residues6
Detailsbinding site for residue 7FF D 1103
ChainResidue
DALA923
DVAL928
DPRO929
DPHE979
DASN980
DHOH1215

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 Residues188
DetailsZN_FING: PHD-type => ECO:0000255|PROSITE-ProRule:PRU00146
ChainResidueDetails
AGLU826-LEU873
BGLU826-LEU873
CGLU826-LEU873
DGLU826-LEU873

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Interaction with histone H3 that is not methylated at 'Lys-4' (H3K4me0)
ChainResidueDetails
AASP827
BASP827
CASP827
DASP827

site_idSWS_FT_FI3
Number of Residues12
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS875
DLYS875
DLYS992
ALYS992
BLYS875
BLYS992
CLYS875
CLYS992

site_idSWS_FT_FI4
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:25218447
ChainResidueDetails
ALYS949
BLYS949
CLYS949
DLYS949

219140

PDB entries from 2024-05-01

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