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1ICI

CRYSTAL STRUCTURE OF A SIR2 HOMOLOG-NAD 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
B0005737cellular_componentcytoplasm
B0006338biological_processchromatin remodeling
B0008270molecular_functionzinc ion binding
B0016740molecular_functiontransferase activity
B0017136molecular_functionNAD-dependent histone deacetylase activity
B0033558molecular_functionprotein lysine deacetylase activity
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 2001
ChainResidue
ACYS124
ACYS127
ACYS145
ACYS148

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 2002
ChainResidue
BCYS124
BCYS127
BCYS145
BCYS148

site_idAC3
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAD A 1001
ChainResidue
AALA21
AGLY22
AGLU26
APHE32
APRO44
AGLN98
AHIS116
AGLY185
ATHR186
ASER187
AVAL190
AASN211
APRO212
AASP213
ALYS228
AALA229
AHOH2018
AHOH2029
AHOH2030
AHOH2032
AHOH2038
AHOH2054
AHOH2055
AHOH2057
AHOH2086
AHOH2097
AHOH2117
AGLY20

site_idAC4
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD B 1002
ChainResidue
BGLY20
BALA21
BGLY22
BGLU26
BPHE32
BPRO44
BGLN98
BHIS116
BGLY185
BTHR186
BSER187
BVAL190
BASN211
BPRO212
BASP213
BLYS228
BALA229
BHOH2011
BHOH2016
BHOH2023
BHOH2033
BHOH2036
BHOH2059
BHOH2081
BHOH2107
BHOH2120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236
ChainResidueDetails
AHIS116
BHIS116

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676
ChainResidueDetails
AGLY20
BALA229
AGLN98
AGLY185
AASN211
AALA229
BGLY20
BGLN98
BGLY185
BASN211

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01121
ChainResidueDetails
ATYR64
AARG67
BTYR64
BARG67

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01121, ECO:0000269|PubMed:11336676, ECO:0000269|PubMed:12091395
ChainResidueDetails
ACYS124
ACYS127
ACYS145
ACYS148
BCYS124
BCYS127
BCYS145
BCYS148

222036

PDB entries from 2024-07-03

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