Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1S7G

Structural Basis for the Mechanism and Regulation of Sir2 Enzymes

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0006338	biological_process	chromatin remodeling
A	0008270	molecular_function	zinc ion binding
A	0016740	molecular_function	transferase activity
A	0017136	molecular_function	histone deacetylase activity, NAD-dependent
A	0034979	molecular_function	NAD-dependent protein lysine deacetylase activity
A	0036054	molecular_function	protein-malonyllysine demalonylase activity
A	0036055	molecular_function	protein-succinyllysine desuccinylase activity
A	0046872	molecular_function	metal ion binding
A	0051287	molecular_function	NAD binding
A	0070403	molecular_function	NAD+ binding
B	0005737	cellular_component	cytoplasm
B	0006338	biological_process	chromatin remodeling
B	0008270	molecular_function	zinc ion binding
B	0016740	molecular_function	transferase activity
B	0017136	molecular_function	histone deacetylase activity, NAD-dependent
B	0034979	molecular_function	NAD-dependent protein lysine deacetylase activity
B	0036054	molecular_function	protein-malonyllysine demalonylase activity
B	0036055	molecular_function	protein-succinyllysine desuccinylase activity
B	0046872	molecular_function	metal ion binding
B	0051287	molecular_function	NAD binding
B	0070403	molecular_function	NAD+ binding
C	0005737	cellular_component	cytoplasm
C	0006338	biological_process	chromatin remodeling
C	0008270	molecular_function	zinc ion binding
C	0016740	molecular_function	transferase activity
C	0017136	molecular_function	histone deacetylase activity, NAD-dependent
C	0034979	molecular_function	NAD-dependent protein lysine deacetylase activity
C	0036054	molecular_function	protein-malonyllysine demalonylase activity
C	0036055	molecular_function	protein-succinyllysine desuccinylase activity
C	0046872	molecular_function	metal ion binding
C	0051287	molecular_function	NAD binding
C	0070403	molecular_function	NAD+ binding
D	0005737	cellular_component	cytoplasm
D	0006338	biological_process	chromatin remodeling
D	0008270	molecular_function	zinc ion binding
D	0016740	molecular_function	transferase activity
D	0017136	molecular_function	histone deacetylase activity, NAD-dependent
D	0034979	molecular_function	NAD-dependent protein lysine deacetylase activity
D	0036054	molecular_function	protein-malonyllysine demalonylase activity
D	0036055	molecular_function	protein-succinyllysine desuccinylase activity
D	0046872	molecular_function	metal ion binding
D	0051287	molecular_function	NAD binding
D	0070403	molecular_function	NAD+ binding
E	0005737	cellular_component	cytoplasm
E	0006338	biological_process	chromatin remodeling
E	0008270	molecular_function	zinc ion binding
E	0016740	molecular_function	transferase activity
E	0017136	molecular_function	histone deacetylase activity, NAD-dependent
E	0034979	molecular_function	NAD-dependent protein lysine deacetylase activity
E	0036054	molecular_function	protein-malonyllysine demalonylase activity
E	0036055	molecular_function	protein-succinyllysine desuccinylase activity
E	0046872	molecular_function	metal ion binding
E	0051287	molecular_function	NAD binding
E	0070403	molecular_function	NAD+ binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 601

Chain	Residue
A	CYS126
A	CYS129
A	CYS150
A	CYS153

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 602

Chain	Residue
A	HIS17
A	GLU180
A	HIS183
C	HIS130

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 603

Chain	Residue
B	CYS129
B	CYS150
B	CYS153
B	CYS126

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 604

Chain	Residue
B	HIS17
B	GLU180
B	HIS183
D	HIS130

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 605

Chain	Residue
C	CYS126
C	CYS129
C	CYS150
C	CYS153

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 606

Chain	Residue
A	HIS130
C	HIS17
C	GLU180
C	HIS183

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 607

Chain	Residue
D	CYS126
D	CYS129
D	CYS150
D	CYS153

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 608

Chain	Residue
B	HIS130
D	HIS17
D	GLU180
D	HIS183

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 609

Chain	Residue
E	CYS126
E	CYS129
E	CYS150
E	CYS153

site_id	BC1
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 A 401

Chain	Residue
A	PRO170
A	GLN171
A	ARG172
A	THR173
A	HOH757
C	LEU169
C	PRO170
C	GLN171
C	ARG172

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE SO4 B 402

Chain	Residue
B	PRO170
B	GLN171
B	ARG172
B	THR173
B	HOH711
B	HOH723
D	PRO170
D	GLN171
D	ARG172

site_id	BC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 D 403

Chain	Residue
D	ARG161

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 B 404

Chain	Residue
B	LYS123
B	THR132
B	ARG161

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 405

Chain	Residue
A	LYS123
A	ARG161

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 406

Chain	Residue
C	LYS123
C	THR132
C	ARG161

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 407

Chain	Residue
A	MET91
A	LYS247
A	ARG250
D	ARG90

site_id	BC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 D 408

Chain	Residue
D	ALA24
D	GLY25
D	GLY191
D	SER192
D	SER193

site_id	BC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 409

Chain	Residue
B	ARG6
B	LYS7

site_id	CC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE SO4 B 410

Chain	Residue
B	ARG149

site_id	CC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 411

Chain	Residue
C	LYS144
C	ARG149

site_id	CC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 412

Chain	Residue
A	LYS57
C	LYS182

site_id	CC4
Number of Residues	25
Details	BINDING SITE FOR RESIDUE NAD B 701

Chain	Residue
B	ALA235
B	HOH705
B	HOH728
B	HOH741
B	HOH749
B	GLY23
B	ALA24
B	GLY25
B	GLU29
B	ILE32
B	THR34
B	PHE35
B	ARG36
B	GLN100
B	ASN101
B	ILE102
B	ASP103
B	HIS118
B	GLY191
B	SER193
B	ASN217
B	ALA218
B	GLU219
B	GLY233
B	LYS234

site_id	CC5
Number of Residues	27
Details	BINDING SITE FOR RESIDUE NAD C 702

Chain	Residue
C	GLY23
C	ALA24
C	GLY25
C	ALA28
C	GLU29
C	ILE32
C	PRO33
C	THR34
C	PHE35
C	ARG36
C	GLN100
C	ASN101
C	ILE102
C	ASP103
C	HIS118
C	GLY191
C	SER192
C	SER193
C	ASN217
C	ALA218
C	GLU219
C	GLY233
C	LYS234
C	ALA235
C	HOH703
C	HOH707
C	HOH738

site_id	CC6
Number of Residues	19
Details	BINDING SITE FOR RESIDUE NAD A 703

Chain	Residue
A	GLY23
A	ALA24
A	GLY25
A	GLU29
A	THR34
A	GLN100
A	GLY191
A	SER192
A	SER193
A	ASN217
A	ALA218
A	GLU219
A	GLY233
A	LYS234
A	ALA235
A	HOH743
A	HOH755
A	HOH760
A	HOH762

site_id	CC7
Number of Residues	20
Details	BINDING SITE FOR RESIDUE APR E 704

Chain	Residue
E	GLY23
E	ALA24
E	GLY25
E	ALA28
E	GLU29
E	THR34
E	PHE35
E	ARG36
E	TRP42
E	GLN100
E	HIS118
E	PHE165
E	GLY191
E	SER192
E	SER193
E	ASN217
E	ALA218
E	GLU219
E	LYS234
E	ALA235

site_id	CC8
Number of Residues	13
Details	BINDING SITE FOR RESIDUE 2PE B 501

Chain	Residue
B	ALA51
B	PHE66
B	SER67
B	ILE102
B	MET104
B	ARG108
B	HIS118
B	VAL163
B	PHE165
B	LEU169
B	VAL196
B	TYR197
B	HOH760

site_id	CC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE P6G C 502

Chain	Residue
C	SER67
C	ILE102
C	HIS118
C	VAL163
C	HOH751

site_id	DC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PG4 D 503

Chain	Residue
D	PHE66
D	VAL163

site_id	DC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 1PE A 504

Chain	Residue
A	PHE63
A	SER67
A	LEU74
A	MET121
A	EDO505

site_id	DC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO A 505

Chain	Residue
A	1PE504

site_id	DC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PG4 C 506

Chain	Residue
C	ARG61
C	ARG61
C	LYS144
C	TYR156
C	HOH724

site_id	DC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO B 508

Chain	Residue
B	VAL162
B	VAL163
B	GLU167
B	PRO168
D	GLN171
D	ARG172
D	HOH609

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	753
Details	Domain: {"description":"Deacetylase sirtuin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	5
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	136
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01121","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15023335","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15780941","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)