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6HSK

Crystal structure of a human HDAC8 L6 loop mutant complexed with Quisinostat

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
B0000118cellular_componenthistone deacetylase complex
B0000122biological_processnegative regulation of transcription by RNA polymerase II
B0000228cellular_componentnuclear chromosome
B0004407molecular_functionhistone deacetylase activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005694cellular_componentchromosome
B0005737cellular_componentcytoplasm
B0006325biological_processchromatin organization
B0007064biological_processmitotic sister chromatid cohesion
B0016787molecular_functionhydrolase activity
B0030544molecular_functionHsp70 protein binding
B0031397biological_processnegative regulation of protein ubiquitination
B0031647biological_processregulation of protein stability
B0032204biological_processregulation of telomere maintenance
B0033558molecular_functionprotein lysine deacetylase activity
B0040029biological_processepigenetic regulation of gene expression
B0046872molecular_functionmetal ion binding
B0051879molecular_functionHsp90 protein binding
B0140297molecular_functionDNA-binding transcription factor binding
B0160008molecular_functionprotein decrotonylase activity
B0160009molecular_functionhistone decrotonylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
AASP178
AHIS180
AASP267
AGOK404

site_idAC2
Number of Residues5
Detailsbinding site for residue K A 402
ChainResidue
AASP176
AASP178
AHIS180
ASER199
ALEU200

site_idAC3
Number of Residues6
Detailsbinding site for residue K A 403
ChainResidue
APHE189
ATHR192
AVAL195
ATYR225
AHOH512
AHOH611

site_idAC4
Number of Residues14
Detailsbinding site for residue GOK A 404
ChainResidue
AHIS142
AHIS143
AGLY151
APHE152
AARG167
AASP178
AHIS180
AGLY206
APHE208
APRO209
AASP267
ATYR306
AZN401
AHOH629

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BASP178
BHIS180
BASP267
BGOK404

site_idAC6
Number of Residues5
Detailsbinding site for residue K B 402
ChainResidue
BASP176
BASP178
BHIS180
BSER199
BLEU200

site_idAC7
Number of Residues6
Detailsbinding site for residue K B 403
ChainResidue
BPHE189
BTHR192
BVAL195
BTYR225
BHOH518
BHOH621

site_idAC8
Number of Residues16
Detailsbinding site for residue GOK B 404
ChainResidue
BHIS142
BHIS143
BGLY151
BPHE152
BARG167
BASP178
BHIS180
BGLY206
BPHE208
BPRO209
BASP267
BTYR306
BZN401
BHOH502
BHOH646
BHOH672

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:19053282
ChainResidueDetails
AHIS143
BHIS143

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:19053282
ChainResidueDetails
AASP101
AGLY151
ATYR306
BASP101
BGLY151
BTYR306

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:17721440
ChainResidueDetails
AASP178
AHIS180
AASP267
BASP178
BHIS180
BASP267

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15242608
ChainResidueDetails
ASER39
BSER39

226707

PDB entries from 2024-10-30

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