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2VQM

Structure of HDAC4 catalytic domain bound to a hydroxamic acid inhbitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0000118cellular_componenthistone deacetylase complex
A0004407molecular_functionhistone deacetylase activity
A0006325biological_processchromatin organization
A0016575biological_processhistone deacetylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A1408
ChainResidue
AASP194
AASP196
AHIS198
ASER217
ALEU218

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A1409
ChainResidue
AHOH2235
AHOH2236
APHE207
AASP210
AVAL213
APHE244

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE HA3 A1410
ChainResidue
ALEU78
ATYR79
AVAL121
AALA124
APRO156
AGLY167
APHE168
AHIS198
APHE227
AASP290
AGLY330
AZN1411
AHOH2296
AHOH2372
AHOH2373
AHOH2375

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A1411
ChainResidue
AASP196
AHIS198
AASP290
AHA31410
AHOH2375

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A1412
ChainResidue
AHIS21
ACYS23
AHIS34
ACYS107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AHIS159

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ACYS23
ACYS25
AHIS31
ACYS107

218853

PDB entries from 2024-04-24

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