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7LTK

STRUCTURE OF HUMAN HDAC2 IN COMPLEX WITH AN INHIBITOR THAT LACKS A ZINC BINDING GROUP (COMPOUND 12)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004407molecular_functionhistone deacetylase activity
B0004407molecular_functionhistone deacetylase activity
C0004407molecular_functionhistone deacetylase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q13547
ChainResidueDetails
BHIS142
CHIS142
AHIS142

site_idSWS_FT_FI2
Number of Residues27
DetailsBINDING: BINDING => ECO:0000269|PubMed:37137925, ECO:0007744|PDB:8BPA, ECO:0007744|PDB:8BPB, ECO:0007744|PDB:8BPC
ChainResidueDetails
APHE188
ATHR191
AVAL194
ASER198
APHE199
AASP265
BASP175
BASP177
BHIS179
BPHE188
BTHR191
BVAL194
BSER198
BPHE199
BASP265
CASP175
CASP177
CHIS179
CPHE188
CTHR191
CVAL194
CSER198
CPHE199
CASP265
AASP177
AHIS179
AASP175

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:37137925, ECO:0007744|PDB:8BPB, ECO:0007744|PDB:8BPC
ChainResidueDetails
BTYR223
CTYR223
ATYR223

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:Q13547
ChainResidueDetails
CLYS75
ALYS75
BLYS75

site_idSWS_FT_FI5
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q13547
ChainResidueDetails
BLYS221
CLYS221
ALYS221

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:P70288
ChainResidueDetails
ACYS262
ACYS274
BCYS262
BCYS274
CCYS262
CCYS274

site_idSWS_FT_FI7
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS75
BLYS75
CLYS75

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PDB entries from 2024-05-29

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