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1M2H

Sir2 homologue S24A mutant-ADP ribose complex

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
A0036054molecular_functionprotein-malonyllysine demalonylase activity
A0036055molecular_functionprotein-succinyllysine desuccinylase activity
A0046872molecular_functionmetal ion binding
A0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 999
ChainResidue
ACYS124
ACYS127
ACYS145
ACYS148
ASER150

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE APR A 1001
ChainResidue
ATHR31
APHE32
AARG33
ATRP39
AGLN98
AHIS116
APHE159
AGLY185
ATHR186
ASER187
AVAL190
AASN211
APRO212
AASP213
ALYS228
AALA229
AHOH1011
AHOH1105
AHOH1160
AHOH1162
AHOH1174
AGLY20
AALA21
AGLY22
AGLU26

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236
ChainResidueDetails
AHIS116

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676
ChainResidueDetails
AGLY20
AGLN98
AGLY185
AASN211
AALA229

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01121
ChainResidueDetails
ATYR64
AARG67

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395
ChainResidueDetails
ACYS124
ACYS127
ACYS145
ACYS148

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PDB entries from 2024-05-01

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