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1M2N

Sir2 homologues (D102G/F159A/R170A) mutant-2'-O-acetyl ADP ribose complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0006338biological_processchromatin remodeling
A0008270molecular_functionzinc ion binding
A0016740molecular_functiontransferase activity
A0017136molecular_functionhistone deacetylase activity, NAD-dependent
A0034979molecular_functionNAD-dependent protein lysine deacetylase activity
A0036054molecular_functionprotein-malonyllysine demalonylase activity
A0036055molecular_functionprotein-succinyllysine desuccinylase activity
A0046872molecular_functionmetal ion binding
A0070403molecular_functionNAD+ binding
B0005737cellular_componentcytoplasm
B0006338biological_processchromatin remodeling
B0008270molecular_functionzinc ion binding
B0016740molecular_functiontransferase activity
B0017136molecular_functionhistone deacetylase activity, NAD-dependent
B0034979molecular_functionNAD-dependent protein lysine deacetylase activity
B0036054molecular_functionprotein-malonyllysine demalonylase activity
B0036055molecular_functionprotein-succinyllysine desuccinylase activity
B0046872molecular_functionmetal ion binding
B0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 999
ChainResidue
ACYS124
ACYS127
ACYS145
ACYS148

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 999
ChainResidue
BCYS124
BCYS127
BCYS145
BCYS148
BSER150

site_idAC3
Number of Residues21
DetailsBINDING SITE FOR RESIDUE OAD B 1001
ChainResidue
AGLY20
AALA21
AGLY22
AGLU26
ATHR31
APHE32
AARG33
AGLN98
AHIS116
AVAL157
AGLY185
ATHR186
ASER187
AVAL190
AASN211
APRO212
ALYS228
AALA229
ALYS247
BHOH2002
BHOH2087

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE OAD B 2001
ChainResidue
BGLY20
BALA21
BGLY22
BGLU26
BTHR31
BPHE32
BARG33
BGLN98
BHIS116
BVAL157
BGLY185
BTHR186
BSER187
BVAL190
BASN211
BPRO212
BASP213
BLYS228
BALA229
BLYS247
BHOH2003
BHOH2027
BHOH2076

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues484
DetailsDomain: {"description":"Deacetylase sirtuin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues54
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01121","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11336676","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01121","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01121","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11336676","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12091395","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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