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5YQM

Crystal structure of Sirt2 in complex with selective inhibitor A29

Functional Information from GO Data
ChainGOidnamespacecontents
A0017136molecular_functionNAD-dependent histone deacetylase activity
A0051287molecular_functionNAD binding
A0070403molecular_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 Residues13
Detailsbinding site for residue A2X A 402
ChainResidue
ALEU138
ATYR139
APRO140
APHE143
APHE190
AILE232
AVAL233
AHOH565
APHE96
AILE118
APHE119
APHE131
AALA135

site_idAC3
Number of Residues5
Detailsbinding site for residue BME A 403
ChainResidue
AGLN72
ALYS158
ATRP337
AHOH631
AHOH744

site_idAC4
Number of Residues1
Detailsbinding site for residue BME A 404
ChainResidue
AARG97

site_idAC5
Number of Residues7
Detailsbinding site for residue BME A 405
ChainResidue
AALA85
AGLN167
AASN168
AILE169
AHOH538
AHOH542
AHOH547

site_idAC6
Number of Residues4
Detailsbinding site for residue BME A 406
ChainResidue
ALYS229
AASP231
AGLU237
AHOH511

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236
ChainResidueDetails
AHIS187

site_idSWS_FT_FI2
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:25672491, ECO:0007744|PDB:4RMG
ChainResidueDetails
AALA85
AASP95
AGLN167
ATHR262
AASN286
ACYS324

site_idSWS_FT_FI3
Number of Residues4
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

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5RJQ4
ChainResidueDetails
ASER100
ASER207

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PDB entries from 2024-07-17

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