Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3F07

Crystal Structure Analysis of Human HDAC8 complexed with APHA in a new monoclinic crystal form

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
A0006338biological_processchromatin remodeling
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
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
B0006338biological_processchromatin remodeling
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
B0046872molecular_functionmetal ion binding
B0051879molecular_functionHsp90 protein binding
B0140297molecular_functionDNA-binding transcription factor binding
B0160008molecular_functionprotein decrotonylase activity
B0160009molecular_functionhistone decrotonylase activity
C0000118cellular_componenthistone deacetylase complex
C0000122biological_processnegative regulation of transcription by RNA polymerase II
C0000228cellular_componentnuclear chromosome
C0004407molecular_functionhistone deacetylase activity
C0005515molecular_functionprotein binding
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005694cellular_componentchromosome
C0005737cellular_componentcytoplasm
C0006325biological_processchromatin organization
C0006338biological_processchromatin remodeling
C0007064biological_processmitotic sister chromatid cohesion
C0016787molecular_functionhydrolase activity
C0030544molecular_functionHsp70 protein binding
C0031397biological_processnegative regulation of protein ubiquitination
C0031647biological_processregulation of protein stability
C0032204biological_processregulation of telomere maintenance
C0033558molecular_functionprotein lysine deacetylase activity
C0046872molecular_functionmetal ion binding
C0051879molecular_functionHsp90 protein binding
C0140297molecular_functionDNA-binding transcription factor binding
C0160008molecular_functionprotein decrotonylase activity
C0160009molecular_functionhistone decrotonylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
AASP178
AHIS180
AASP267
AAGE500

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 401
ChainResidue
AASP176
AASP178
AHIS180
ASER199
ALEU200

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 402
ChainResidue
APHE189
ATHR192
AVAL195
ATYR225
ASER226

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 409
ChainResidue
AHIS78
AASP87
AHIS90
AASP92
ASER93

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE AGE A 500
ChainResidue
ALYS33
AASP101
AHIS142
AHIS143
AASP178
AHIS180
AGLY206
APHE208
AASP267
AMET274
ATYR306
AZN400

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 403
ChainResidue
BASP178
BHIS180
BASP267
BAGE501

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 404
ChainResidue
BASP176
BASP178
BHIS180
BSER199
BLEU200

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 405
ChainResidue
BPHE189
BTHR192
BVAL195
BTYR225
BSER226

site_idAC9
Number of Residues13
DetailsBINDING SITE FOR RESIDUE AGE B 501
ChainResidue
BLYS33
BASP101
BHIS142
BHIS143
BPHE152
BASP178
BHIS180
BPHE207
BPHE208
BMET274
BGLY304
BTYR306
BZN403

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 406
ChainResidue
CASP178
CHIS180
CASP267
CHOH813

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K C 407
ChainResidue
CASP176
CASP178
CHIS180
CSER199
CLEU200

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K C 408
ChainResidue
CPHE189
CTHR192
CVAL195
CTYR225
CSER226

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:19053282
ChainResidueDetails
AHIS143
BHIS143
CHIS143

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:19053282
ChainResidueDetails
AASP101
AGLY151
ATYR306
BASP101
BGLY151
BTYR306
CASP101
CGLY151
CTYR306

site_idSWS_FT_FI3
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:17721440
ChainResidueDetails
AASP178
AHIS180
AASP267
BASP178
BHIS180
BASP267
CASP178
CHIS180
CASP267

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:15242608
ChainResidueDetails
ASER39
BSER39
CSER39

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon