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4RMJ

Human Sirt2 in complex with ADP ribose and nicotinamide

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 Residues24
DetailsBINDING SITE FOR RESIDUE AR6 A 401
ChainResidue
AGLY84
AHIS187
APHE235
AGLY261
ATHR262
ASER263
AASN286
ALYS287
AGLU288
AGLY322
AGLU323
AALA85
ACYS324
AEDO404
AHOH504
AHOH543
AHOH549
AGLY86
ATHR89
AASP95
APHE96
AARG97
ATYR104
AGLN167

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NCA A 402
ChainResidue
AILE93
APRO94
APHE96
AASN168
AILE169
AASP170

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PEG A 403
ChainResidue
AGLU56
ASER100
ATHR101
AASN106
APRO277
ALEU278
ASER279

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 404
ChainResidue
APHE119
AHIS187
AVAL233
AAR6401

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 405
ChainResidue
ASER88
AHIS149
AASN168
AASP170
AGLU173

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 406
ChainResidue
ACYS195
ACYS200
ACYS221
ACYS224

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 401
ChainResidue
BCYS195
BCYS200
BCYS221
BCYS224

site_idAC8
Number of Residues24
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
BEDO404
BHOH514
BHOH526

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE EDO B 403
ChainResidue
BLEU321

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 404
ChainResidue
BHIS187
BVAL233
BAR6402
BHOH520

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PGE B 405
ChainResidue
BGLN265
BGLY291
BSER293
BPHE296
BMET299
BILE300
BMET301
BGLY304
BHOH519

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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