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2H2H

The Structural basis of sirtuin substrate specificity

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006338biological_processchromatin remodeling
A0008270molecular_functionzinc ion binding
A0016740molecular_functiontransferase activity
A0017136molecular_functionNAD-dependent histone 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
DetailsMOD_RES: N6-succinyllysine => ECO:0000269|PubMed:22389435
ChainResidueDetails
BARG10

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:16768447
ChainResidueDetails
BTHR12
AGLY216
AASP231
AVAL232
ATHR26
AARG34
AGLN98
AHIS116
ASER189
ASER190
AASN214
ALEU215

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

223532

PDB entries from 2024-08-07

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