5YQL

Crystal structure of Sirt2 in complex with selective inhibitor A2I

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	15
Details	binding site for residue A2I A 1001

Chain	Residue
A	PHE96
A	PHE190
A	LEU206
A	ILE232
A	VAL233
A	PHE234
A	HOH1322
A	PHE119
A	PHE131
A	ALA135
A	LEU138
A	TYR139
A	PRO140
A	PHE143
A	ASP170

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site_id	AC2
Number of Residues	4
Details	binding site for residue ZN A 1002

Chain	Residue
A	CYS195
A	CYS200
A	CYS221
A	CYS224

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site_id	AC3
Number of Residues	5
Details	binding site for residue BME A 1003

Chain	Residue
A	TRP320
A	LEU321
A	HOH1237
A	HOH1336
A	HOH1472

---

site_id	AC4
Number of Residues	6
Details	binding site for residue BME A 1004

Chain	Residue
A	GLY84
A	ALA85
A	GLN167
A	THR262
A	SER263
A	HOH1288

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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

---

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	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5RJQ4

Chain	Residue	Details
A	SER100
A	SER207

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