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4R8M

Human SIRT2 crystal structure in complex with BHJH-TM1

Functional Information from GO Data
ChainGOidnamespacecontents
A0017136molecular_functionNAD-dependent histone deacetylase activity
A0051287molecular_functionNAD binding
A0070403molecular_functionNAD+ binding
B0017136molecular_functionNAD-dependent histone deacetylase activity
B0051287molecular_functionNAD binding
B0070403molecular_functionNAD+ binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 401
ChainResidue
ACYS195
ACYS200
ACYS221
ACYS224

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 401
ChainResidue
BCYS195
BCYS200
BCYS221
BCYS224

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE 3LX C 600
ChainResidue
APHE119
AHIS187
APHE190
AILE232
CLYS3
AARG97

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE 3LX D 600
ChainResidue
BPHE119
BILE169
BHIS187
DLYS3

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236
ChainResidueDetails
AHIS187
BHIS187

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:25672491, ECO:0007744|PDB:4RMG
ChainResidueDetails
AALA85
BTHR262
BASN286
BCYS324
AASP95
AGLN167
ATHR262
AASN286
ACYS324
BALA85
BASP95
BGLN167

site_idSWS_FT_FI3
Number of Residues8
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00236, ECO:0000269|PubMed:11427894, ECO:0000269|PubMed:23454361, ECO:0000269|PubMed:24389023, ECO:0000269|PubMed:25672491, ECO:0000269|PubMed:25704306, ECO:0007744|PDB:4R8M
ChainResidueDetails
ACYS195
ACYS200
ACYS221
ACYS224
BCYS195
BCYS200
BCYS221
BCYS224

site_idSWS_FT_FI4
Number of Residues6
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5RJQ4
ChainResidueDetails
ASER53
ASER100
ASER207
BSER53
BSER100
BSER207

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PDB entries from 2024-07-24

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