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2VQW

Structure of inhibitor-free HDAC4 catalytic domain (with gain-of- function mutation His332Tyr)

Functional Information from GO Data
ChainGOidnamespacecontents
G0000118cellular_componenthistone deacetylase complex
G0004407molecular_functionhistone deacetylase activity
G0006325biological_processchromatin organization
G0016575biological_processhistone deacetylation
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K G1407
ChainResidue
GASP194
GASP196
GHIS198
GSER217
GLEU218

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE K G1408
ChainResidue
GPHE207
GASP210
GVAL213
GPHE244

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN G1409
ChainResidue
GASP196
GHIS198
GASP290

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN G1410
ChainResidue
GCYS23
GCYS25
GHIS31
GCYS107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
GHIS159

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
GCYS23
GCYS25
GHIS31
GCYS107

218196

PDB entries from 2024-04-10

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