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4QA4

Crystal structure of H334R HDAC8 in complex with M344

Functional Information from GO Data
ChainGOidnamespacecontents
A0000118cellular_componenthistone deacetylase complex
A0000122biological_processnegative regulation of transcription by RNA polymerase II
A0000228cellular_componentnuclear chromosome
A0004407molecular_functionhistone deacetylase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0006325biological_processchromatin organization
A0007064biological_processmitotic sister chromatid cohesion
A0016787molecular_functionhydrolase activity
A0030544molecular_functionHsp70 protein binding
A0031397biological_processnegative regulation of protein ubiquitination
A0031647biological_processregulation of protein stability
A0032204biological_processregulation of telomere maintenance
A0033558molecular_functionprotein lysine deacetylase activity
A0040029biological_processepigenetic regulation of gene expression
A0046872molecular_functionmetal ion binding
A0051879molecular_functionHsp90 protein binding
A0140297molecular_functionDNA-binding transcription factor binding
A0160008molecular_functionprotein decrotonylase activity
A0160009molecular_functionhistone decrotonylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE B3N A 501
ChainResidue
ATYR100
APRO273
AMET274
ATYR306
ATYR306
AZN502
AHOH702
AASP101
AHIS142
AHIS143
AGLY151
APHE152
AASP178
AHIS180
AASP267

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 502
ChainResidue
AASP178
AHIS180
AASP267
AB3N501

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 503
ChainResidue
AASP176
AASP178
AHIS180
ASER199
ALEU200

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 504
ChainResidue
APHE189
ATHR192
AVAL195
ATYR225
AHOH604
AHOH608

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 505
ChainResidue
AGLN236
ASER351
ACYS352
AARG353

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 506
ChainResidue
ALYS289
ATYR317
AVAL321
AGLY324
ALYS325
ATHR326
AHOH617

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL A 507
ChainResidue
ASER215
AASP216
AVAL217
AGLY218
AARG223

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:19053282
ChainResidueDetails
AHIS143

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:19053282
ChainResidueDetails
AASP101
AGLY151
ATYR306

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:17721440
ChainResidueDetails
AASP267
AASP178
AHIS180

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15242608
ChainResidueDetails
ASER39

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PDB entries from 2024-05-29

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