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5D7P

Crystal structure of human Sirt2 in complex with ADPR and EX-243

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 Residues26
Detailsbinding site for residue AR6 A 402
ChainResidue
APHE96
AARG97
ATYR104
AGLN167
AHIS187
APHE235
AGLY261
ATHR262
ASER263
AVAL266
AASN286
ALYS287
AGLU288
AGLY322
AGLU323
ACYS324
AOCZ404
AHOH537
AHOH543
AHOH545
AHOH566
AGLY84
AALA85
AGLY86
ATHR89
AASP95

site_idAC3
Number of Residues8
Detailsbinding site for residue OCZ A 403
ChainResidue
APHE131
ALEU138
ATYR139
APRO140
AGLY141
APHE190
AOCZ404
AHOH551

site_idAC4
Number of Residues11
Detailsbinding site for residue OCZ A 404
ChainResidue
APRO94
APHE96
APHE119
AGLN167
AASN168
AILE169
AASP170
AILE232
AAR6402
AOCZ403
AHOH558

site_idAC5
Number of Residues4
Detailsbinding site for residue ZN B 401
ChainResidue
BCYS195
BCYS200
BCYS221
BCYS224

site_idAC6
Number of Residues25
Detailsbinding site for residue AR6 B 402
ChainResidue
BGLY84
BALA85
BGLY86
BTHR89
BASP95
BPHE96
BARG97
BTYR104
BGLN167
BHIS187
BPHE235
BGLY261
BTHR262
BSER263
BVAL266
BASN286
BLYS287
BGLU288
BGLY322
BGLU323
BCYS324
BOCZ404
BHOH504
BHOH507
BHOH521

site_idAC7
Number of Residues7
Detailsbinding site for residue OCZ B 403
ChainResidue
BPHE131
BALA135
BLEU138
BTYR139
BGLY141
BPHE190
BOCZ404

site_idAC8
Number of Residues10
Detailsbinding site for residue OCZ B 404
ChainResidue
BPHE96
BPHE119
BGLN167
BASN168
BILE169
BASP170
BILE232
BAR6402
BOCZ403
BHOH569

site_idAC9
Number of Residues8
Detailsbinding site for residue PEG B 405
ChainResidue
BSER98
BLYS287
BHOH503
BHOH529
BTHR89
BILE93
BPRO94
BASP95

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 Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5RJQ4
ChainResidueDetails
ASER100
ASER207
BSER100
BSER207

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PDB entries from 2024-07-24

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