1SZD

Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD+-dependent Sir2 histone/protein deacetylases

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0017136	molecular_function	histone deacetylase activity, NAD-dependent
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 701

Chain	Residue
A	CYS143
A	CYS146
A	CYS170
A	CYS173

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site_id	AC2
Number of Residues	32
Details	BINDING SITE FOR RESIDUE APR A 1001

Chain	Residue
A	ARG45
A	GLU64
A	GLN115
A	GLY223
A	THR224
A	SER225
A	VAL228
A	ASN248
A	LEU249
A	GLN268
A	TYR269
A	SER270
A	HOH1999
A	HOH2003
A	HOH2010
A	HOH2015
A	HOH2042
A	HOH2133
A	HOH2134
A	HOH2135
A	HOH2147
A	HOH2153
A	HOH2162
A	HOH2239
A	HOH2311
B	ALY16
B	HIS18
A	GLY32
A	ALA33
A	GLY34
A	THR37
A	PHE44

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1989

Chain	Residue
A	SER193
A	TRP196
A	GLU237
A	HOH2005
B	LYS12

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site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE GOL A 1990

Chain	Residue
A	GLY50
A	HOH2142

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site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1991

Chain	Residue
A	LYS84
A	TYR87
A	ASN90
A	LEU159
A	ALA160

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Functional Information from PROSITE/UniProt

site_id	PS00047
Number of Residues	5
Details	HISTONE_H4 Histone H4 signature. GAKRH

Chain	Residue	Details
B	GLY14-HIS18

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20726530","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14502267","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15150415","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14502267","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14604530","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15150415","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17289592","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"22343720","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"11080160","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15150415","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17289592","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19113941","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	8
Details

Chain	Residue	Details
A	ASP118
A	PHE44
A	PHE44
A	PRO42
A	HIS135
A	ASP43
A	ARG45
A	ASN116

---

site_id	MCSA1
Number of Residues	7
Details	M-CSA 240

Chain	Residue	Details
A	PRO42	hydrogen bond acceptor, steric role
A	ASP43	hydrogen bond acceptor, hydrogen bond donor, steric role
A	PHE44	steric role, van der waals interaction
A	ARG45	electrostatic stabiliser, hydrogen bond donor
A	ASN116	activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity
A	ASP118	activator, hydrogen bond acceptor
A	HIS135	hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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