4X3P

Sirt2 in complex with a myristoyl peptide

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0017136	molecular_function	NAD-dependent histone deacetylase activity
A	0051287	molecular_function	NAD binding
A	0070403	molecular_function	NAD+ binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 401

Chain	Residue
A	CYS195
A	CYS200
A	CYS221
A	CYS224

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site_id	AC2
Number of Residues	2
Details	binding site for residue EDO A 402

Chain	Residue
A	TRP320
A	LEU321

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site_id	AC3
Number of Residues	26
Details	binding site for residue CNA A 403

Chain	Residue
A	THR89
A	PRO94
A	ASP95
A	PHE96
A	ARG97
A	GLN167
A	ASN168
A	ILE169
A	ASP170
A	HIS187
A	GLY261
A	THR262
A	SER263
A	ASN286
A	LYS287
A	GLU288
A	GLY322
A	GLU323
A	CYS324
A	HOH552
A	HOH564
A	HOH622
C	3LX101
A	GLY84
A	ALA85
A	GLY86

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site_id	AC4
Number of Residues	5
Details	binding site for residue 3LX C 101

Chain	Residue
A	PHE96
A	LEU138
A	VAL233
A	CNA403
C	LYS9

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236

Chain	Residue	Details
A	HIS187

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site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000269|PubMed:25672491, ECO:0007744|PDB:4RMG

Chain	Residue	Details
A	ALA85
A	ASP95
A	GLN167
A	THR262
A	ASN286
A	CYS324

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site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: 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

Chain	Residue	Details
A	CYS195
A	CYS200
A	CYS221
A	CYS224

---

site_id	SWS_FT_FI4
Number of Residues	3
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5RJQ4

Chain	Residue	Details
A	SER53
A	SER100
A	SER207

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