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4RMG

Human Sirt2 in complex with SirReal2 and NAD+

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 Residues14
DetailsBINDING SITE FOR RESIDUE 3TE A 402
ChainResidue
ATYR139
APRO140
AASP170
APHE190
AILE232
AVAL233
APHE234
AMET299
AHOH540
APHE96
AILE118
APHE119
APHE131
AALA135

site_idAC3
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD A 403
ChainResidue
AGLY84
AALA85
AGLY86
ATHR89
AILE93
APRO94
AASP95
APHE96
AGLN167
AASN168
AILE169
AASP170
AHIS187
AGLY261
ATHR262
ASER263
AASN286
ALYS287
AGLU288
AMET299
AGLY322
AGLU323
ACYS324
AHOH501
AHOH502
AHOH558

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

223790

PDB entries from 2024-08-14

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