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3JR3

Sir2 bound to acetylated peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006338biological_processchromatin remodeling
A0008270molecular_functionzinc ion binding
A0016740molecular_functiontransferase activity
A0017136molecular_functionNAD-dependent histone deacetylase activity
A0033558molecular_functionprotein lysine deacetylase activity
A0034979molecular_functionNAD-dependent protein lysine deacetylase activity
A0046872molecular_functionmetal ion binding
A0051287molecular_functionNAD binding
A0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 1001
ChainResidue
ACYS124
ACYS127
ACYS148
ACYS151

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:16905097
ChainResidueDetails
AALA116

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:16905097, ECO:0007744|PDB:2H4F
ChainResidueDetails
AGLY216
AASP231
AVAL232
AALA22
ATHR26
AARG34
AGLN98
AALA116
ASER189
ASER190
ALEU215
AASN214

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:15780941, ECO:0007744|PDB:1YC5
ChainResidueDetails
APHE33
AILE100
AASP101

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:15780941, ECO:0000269|PubMed:16768447, ECO:0000269|PubMed:16905097, ECO:0000269|PubMed:18786399, ECO:0000269|PubMed:19801667, ECO:0000269|PubMed:21080423, ECO:0007744|PDB:1YC5, ECO:0007744|PDB:2H2D, ECO:0007744|PDB:2H4F, ECO:0007744|PDB:3D4B, ECO:0007744|PDB:3JR3, ECO:0007744|PDB:3PDH
ChainResidueDetails
ACYS124
ACYS127
ACYS148
ACYS151

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PDB entries from 2024-06-12

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