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5YTK

Crystal structure of SIRT3 bound to a leucylated AceCS2

Functional Information from GO Data
ChainGOidnamespacecontents
A0017136molecular_functionNAD-dependent histone deacetylase activity
A0051287molecular_functionNAD binding
A0070403molecular_functionNAD+ binding
B0017136molecular_functionNAD-dependent histone deacetylase activity
B0051287molecular_functionNAD binding
B0070403molecular_functionNAD+ binding
C0017136molecular_functionNAD-dependent histone deacetylase activity
C0051287molecular_functionNAD binding
C0070403molecular_functionNAD+ binding
D0017136molecular_functionNAD-dependent histone deacetylase activity
D0051287molecular_functionNAD binding
D0070403molecular_functionNAD+ binding
E0017136molecular_functionNAD-dependent histone deacetylase activity
E0051287molecular_functionNAD binding
E0070403molecular_functionNAD+ binding
F0017136molecular_functionNAD-dependent histone deacetylase activity
F0051287molecular_functionNAD binding
F0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
ACYS256
ACYS259
ACYS280
ACYS283

site_idAC2
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BCYS256
BCYS259
BCYS280
BCYS283

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN C 401
ChainResidue
CCYS259
CCYS280
CCYS283
CCYS256

site_idAC4
Number of Residues4
Detailsbinding site for residue ZN D 401
ChainResidue
DCYS256
DCYS259
DCYS280
DCYS283

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN E 401
ChainResidue
ECYS256
ECYS259
ECYS280
ECYS283

site_idAC6
Number of Residues4
Detailsbinding site for residue ZN F 401
ChainResidue
FCYS256
FCYS259
FCYS280
FCYS283

site_idAC7
Number of Residues7
Detailsbinding site for Di-peptide LEU B 402 and LYS B 403
ChainResidue
BPHE157
BARG158
BHIS248
BVAL292
BPHE294
BGLY295
BGLU296

site_idAC8
Number of Residues6
Detailsbinding site for Di-peptide LEU C 402 and LYS C 403
ChainResidue
CGLN228
CHIS248
CVAL292
CPHE293
CGLY295
CGLU296

site_idAC9
Number of Residues9
Detailsbinding site for Di-peptide LEU G 701 and LYS G 642
ChainResidue
APHE180
AGLN228
AHIS248
AVAL292
APHE294
AGLU296
ALEU298
GGLY641
GVAL643

site_idAD1
Number of Residues9
Detailsbinding site for Di-peptide LEU J 701 and LYS J 642
ChainResidue
DPHE180
DGLN228
DHIS248
DVAL292
DPHE294
DGLU296
DLEU298
JGLY641
JVAL643

site_idAD2
Number of Residues10
Detailsbinding site for Di-peptide LEU K 701 and LYS K 642
ChainResidue
EPHE180
EGLN228
EHIS248
EVAL292
EPHE293
EPHE294
EGLU296
ELEU298
KGLY641
KVAL643

site_idAD3
Number of Residues7
Detailsbinding site for Di-peptide LEU L 701 and LYS L 642
ChainResidue
FGLN228
FHIS248
FVAL292
FPHE294
FGLU296
LGLY641
LVAL643

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:16788062
ChainResidueDetails
EHIS248
FHIS248
GLYS642
JLYS642
KLYS642
LLYS642

site_idSWS_FT_FI2
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:23897466
ChainResidueDetails
BGLY319
BASN344
CGLY145
CGLN228
CGLY319
CASN344
DGLY145
DGLN228
DGLY319
DASN344
EGLY145
EGLN228
EGLY319
EASN344
FGLY145
FGLN228
FGLY319
FASN344
AGLY145
AGLN228
AGLY319
AASN344
BGLY145
BGLN228

site_idSWS_FT_FI3
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:19535340, ECO:0000269|PubMed:23897466
ChainResidueDetails
ACYS256
ACYS259
ACYS280
ACYS283
BCYS256
BCYS259
BCYS280
BCYS283
CCYS256
CCYS259
CCYS280
CCYS283
DCYS256
DCYS259
DCYS280
DCYS283
ECYS256
ECYS259
ECYS280
ECYS283
FCYS256
FCYS259
FCYS280
FCYS283

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8R104
ChainResidueDetails
ALYS122
BLYS122
CLYS122
DLYS122
ELYS122
FLYS122

219869

PDB entries from 2024-05-15

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