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5DY5

Crystal structure of human Sirt2 in complex with a SirReal probe fragment

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 Residues15
Detailsbinding site for residue 5GR A 402
ChainResidue
ATYR139
APRO140
AILE169
AHIS187
APHE190
AILE232
AVAL233
APHE235
ABU3405
AHOH605
APHE96
AARG97
APHE119
APHE131
AALA135

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 403
ChainResidue
ATHR63
ALEU64
AGLU65
AALA319
AHOH508

site_idAC4
Number of Residues10
Detailsbinding site for residue EPE A 404
ChainResidue
AGLU61
ATHR63
AGLU65
AARG69
AARG78
ALEU252
ALYS253
AVAL254
AASP255
AHOH538

site_idAC5
Number of Residues9
Detailsbinding site for residue BU3 A 405
ChainResidue
AALA85
AASP95
APHE96
AARG97
AGLN167
AASN168
AILE169
A5GR402
AHOH505

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

224201

PDB entries from 2024-08-28

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