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3C10

Crystal structure of catalytic domain of human histone deacetylase HDAC7 in complex with Trichostatin A (TSA)

Replaces:  2PQP
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
ATSN301
AASP707
AHIS709
AASP801

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
AHOH4
AHOH42
APHE718
AASP721
AVAL724
APHE755

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 101
ChainResidue
BTSN301
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
BHOH907
BHOH913

site_idAC9
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN C 101
ChainResidue
CTSN301
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 Residues6
DetailsBINDING SITE FOR RESIDUE K C 202
ChainResidue
CPHE718
CASP721
CVAL724
CPHE755
CHOH906
CHOH913

site_idBC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE TSN A 301
ChainResidue
AZN101
AHOH120
AHOH260
AHIS669
AHIS670
APHE679
AASP707
AHIS709
AASP801
APRO809
ALEU810

site_idBC5
Number of Residues13
DetailsBINDING SITE FOR RESIDUE TSN B 301
ChainResidue
BZN101
BARG540
BASP626
BHIS669
BHIS670
BGLY678
BPHE679
BASP707
BHIS709
BASP801
BLEU810
BGLY841
BHOH953

site_idBC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE TSN C 301
ChainResidue
CZN101
CARG540
CASP626
CHIS669
CHIS670
CPHE679
CASP707
CHIS709
CPHE738
CASP801
CPRO809
CLEU810
CHOH971
CHOH991
CHOH999

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"evidences":[{"source":"UniProtKB","id":"Q8C2B3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18285338","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsSite: {"description":"Contributes to catalysis","evidences":[{"source":"PubMed","id":"18285338","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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