4KXQ

Structure of NAD-dependent protein deacetylase sirtuin-1 (closed state, 1.85 A)

Functional Information from GO Data

Chain	GOid	namespace	contents
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 601

Chain	Residue
A	CYS371
A	CYS374
A	CYS395
A	CYS398

---

site_id	AC2
Number of Residues	27
Details	BINDING SITE FOR RESIDUE APR A 602

Chain	Residue
A	PHE273
A	ARG274
A	TYR280
A	GLN345
A	HIS363
A	PHE414
A	GLY440
A	SER441
A	SER442
A	VAL445
A	ASN465
A	ARG466
A	GLU467
A	GLY480
A	ASP481
A	CYS482
A	HOH712
A	HOH727
A	HOH786
A	HOH802
A	HOH835
A	HOH836
A	GLY261
A	ALA262
A	GLY263
A	VAL266
A	ASP272

---

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BME A 603

Chain	Residue
A	LYS254
A	LYS255
A	GLY337
A	LEU339
A	LEU340
A	HOH744
A	HOH926

---

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE GOL A 604

Chain	Residue
A	ILE270
A	ILE279
A	ILE316
A	ASN346
A	ILE347
A	ASP348
A	HOH733
A	HOH796
A	HOH860
A	HOH866

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	MOD_RES: Phosphoserine; by CaMK2 => ECO:0000250|UniProtKB:Q923E4

Chain	Residue	Details
B	SER659

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine; by CaMK2 => ECO:0000305|PubMed:19236849

Chain	Residue	Details
B	SER661
A	GLN345
A	GLY440
A	ASN465

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00236

Chain	Residue	Details
A	CYS371
A	CYS374
A	CYS395
A	CYS398

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	CYS482

---

site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q923E4

Chain	Residue	Details
A	LYS238
A	LYS377
A	LYS430

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: S-nitrosocysteine => ECO:0000250|UniProtKB:Q923E4

Chain	Residue	Details
A	CYS395
A	CYS398

---