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5TD7

Crystal structure of histone deacetylase 10

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0008270molecular_functionzinc ion binding
A0016236biological_processmacroautophagy
A0016787molecular_functionhydrolase activity
A0019213molecular_functiondeacetylase activity
A0033558molecular_functionprotein lysine deacetylase activity
A0035825biological_processhomologous recombination
A0036269biological_processswimming behavior
A0040029biological_processepigenetic regulation of gene expression
A0046872molecular_functionmetal ion binding
A0047609molecular_functionacetylputrescine deacetylase activity
A0047611molecular_functionacetylspermidine deacetylase activity
A0090043biological_processregulation of tubulin deacetylation
A0106047biological_processpolyamine deacetylation
A0106048biological_processspermidine deacetylation
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 701
ChainResidue
AASP174
AHIS176
AASP267
AFKS711

site_idAC2
Number of Residues5
Detailsbinding site for residue K A 702
ChainResidue
AASP172
AASP174
AHIS176
ASER195
ATRP196

site_idAC3
Number of Residues5
Detailsbinding site for residue K A 703
ChainResidue
APHE185
AASP188
AVAL191
APHE224
AHOH812

site_idAC4
Number of Residues6
Detailsbinding site for residue PO4 A 704
ChainResidue
AGLN56
ALYS106
AHIS201
AASP212
ATYR213
AASN231

site_idAC5
Number of Residues4
Detailsbinding site for residue PO4 A 705
ChainResidue
ALYS528
AGLU575
AARG664
APO4710

site_idAC6
Number of Residues2
Detailsbinding site for residue PO4 A 706
ChainResidue
AARG330
ASER332

site_idAC7
Number of Residues6
Detailsbinding site for residue PO4 A 707
ChainResidue
ALYS75
AGLN76
AGLY79
AGLN346
AASN347
APO4709

site_idAC8
Number of Residues6
Detailsbinding site for residue PO4 A 708
ChainResidue
ALYS75
AHIS201
AASN231
ALYS232
ASER340
AGLU343

site_idAC9
Number of Residues5
Detailsbinding site for residue PO4 A 709
ChainResidue
AGLN76
AMET80
AGLU84
AGLN346
APO4707

site_idAD1
Number of Residues5
Detailsbinding site for residue PO4 A 710
ChainResidue
ASER332
AGLY333
AARG509
AASN577
APO4705

site_idAD2
Number of Residues16
Detailsbinding site for residue FKS A 711
ChainResidue
AASP94
APRO134
AHIS136
AHIS137
AGLY145
APHE146
ACYS147
AASP174
AHIS176
ATRP205
AASP267
AGLU274
AGLU304
AGLY305
APHE307
AZN701

site_idAD3
Number of Residues4
Detailsbinding site for residue 1PE A 712
ChainResidue
AASN545
AASN545
AARG664
AARG664

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:28516954, ECO:0007744|PDB:5TD7
ChainResidueDetails
AHIS137

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:28516954, ECO:0007744|PDB:5TD7
ChainResidueDetails
AASP174
AHIS176
AASP267
APHE307
AASP22
AASP94

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Substrate specificity => ECO:0000269|PubMed:28516954
ChainResidueDetails
AGLU274

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PDB entries from 2024-05-15

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