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6WBQ

Crystal Structure of Danio rerio Histone Deacetylase 10 in Complex with Tubastatin A

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008270molecular_functionzinc ion binding
A0016236biological_processmacroautophagy
A0016787molecular_functionhydrolase activity
A0019213molecular_functiondeacetylase activity
A0035825biological_processhomologous recombination
A0036269biological_processswimming behavior
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 Residues13
Detailsbinding site for residue N9W A 701
ChainResidue
AGLU24
AASP267
AGLU274
ATYR307
AZN712
AALA94
AHIS136
AHIS137
AGLY145
APHE146
AASP174
AHIS176
ATRP205

site_idAC2
Number of Residues9
Detailsbinding site for residue EDO A 702
ChainResidue
AALA2
AVAL119
AARG122
AVAL124
AARG125
AALA296
ALYS298
AHOH818
AHOH828

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 703
ChainResidue
AGLY4
ASER5
AARG125
ALEU323
AHOH962

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 704
ChainResidue
AGLU59
ALEU63
AGLU68
AGLU72

site_idAC5
Number of Residues3
Detailsbinding site for residue EDO A 705
ChainResidue
AASN81
ALYS360
AHIS361

site_idAC6
Number of Residues3
Detailsbinding site for residue EDO A 706
ChainResidue
AARG198
AGLU200
AGLU276

site_idAC7
Number of Residues5
Detailsbinding site for residue K A 707
ChainResidue
AASP172
AASP174
AHIS176
ASER195
ATRP196

site_idAC8
Number of Residues6
Detailsbinding site for residue K A 708
ChainResidue
APHE185
AASP188
AVAL191
APHE224
AHOH887
AHOH971

site_idAC9
Number of Residues10
Detailsbinding site for residue PO4 A 709
ChainResidue
AGLN56
ALYS106
AHIS201
AASP212
ATYR213
AASN231
AHOH806
AHOH813
AHOH816
AHOH916

site_idAD1
Number of Residues7
Detailsbinding site for residue PO4 A 710
ChainResidue
ALYS75
AHIS201
AASN231
ALYS232
ASER340
AGLU343
AHOH913

site_idAD2
Number of Residues4
Detailsbinding site for residue PO4 A 711
ChainResidue
AHIS43
AHIS321
ALYS407
AARG408

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN A 712
ChainResidue
AASP174
AHIS176
AASP267
AN9W701

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsMotif: {"description":"Substrate specificity","evidences":[{"source":"PubMed","id":"28516954","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"28516954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TD7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"28516954","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5TD7","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsSite: {"description":"Substrate specificity","evidences":[{"source":"PubMed","id":"28516954","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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