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3ZNR

HDAC7 bound with inhibitor TMP269

Functional Information from GO Data
ChainGOidnamespacecontents
A0000118cellular_componenthistone deacetylase complex
A0004407molecular_functionhistone deacetylase activity
A0006325biological_processchromatin organization
A0016575biological_processhistone deacetylation
B0000118cellular_componenthistone deacetylase complex
B0004407molecular_functionhistone deacetylase activity
B0006325biological_processchromatin organization
B0016575biological_processhistone deacetylation
C0000118cellular_componenthistone deacetylase complex
C0004407molecular_functionhistone deacetylase activity
C0006325biological_processchromatin organization
C0016575biological_processhistone deacetylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 101
ChainResidue
AASP707
AHIS709
AASP801
ANU91000

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 102
ChainResidue
ACYS533
ACYS535
AHIS541
ACYS618

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 201
ChainResidue
AASP707
AHIS709
ASER728
ALEU729
AASP705

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 202
ChainResidue
APHE718
AASP721
AVAL724
APHE755
AHOH2014
AHOH2015

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN B 101
ChainResidue
BASP707
BHIS709
BASP801

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 102
ChainResidue
BCYS533
BCYS535
BHIS541
BCYS618

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K B 201
ChainResidue
BASP705
BASP707
BHIS709
BSER728
BLEU729

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K B 202
ChainResidue
BPHE718
BASP721
BVAL724
BPHE755
BHOH2017
BHOH2018

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE ZN C 101
ChainResidue
CASP707
CHIS709
CASP801

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 102
ChainResidue
CCYS533
CCYS535
CHIS541
CCYS618

site_idBC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K C 201
ChainResidue
CASP705
CASP707
CHIS709
CSER728
CLEU729

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K C 202
ChainResidue
CPHE718
CVAL724
CPHE755
CHOH2003
CHOH2004

site_idBC4
Number of Residues18
DetailsBINDING SITE FOR RESIDUE NU9 A 1000
ChainResidue
AZN101
APRO542
AGLU543
APRO667
AHIS669
AHIS670
AGLY678
APHE679
ACYS680
AASP707
AHIS709
APHE738
AASP801
APRO809
ALEU810
AGLU840
AGLY841
AHIS843

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q8C2B3
ChainResidueDetails
AHIS670
BHIS670
CHIS670

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:18285338
ChainResidueDetails
ACYS533
CCYS535
CHIS541
CCYS618
ACYS535
AHIS541
ACYS618
BCYS533
BCYS535
BHIS541
BCYS618
CCYS533

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Contributes to catalysis => ECO:0000269|PubMed:18285338
ChainResidueDetails
AHIS843
BHIS843
CHIS843

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER486
BSER486
CSER486

site_idSWS_FT_FI5
Number of Residues9
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER487
ASER507
ASER595
BSER487
BSER507
BSER595
CSER487
CSER507
CSER595

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PDB entries from 2024-07-17

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