4Y6Q

Human SIRT2 in complex with 2-O-myristoyl-ADP-ribose

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
B	0017136	molecular_function	NAD-dependent histone deacetylase activity
B	0051287	molecular_function	NAD binding
B	0070403	molecular_function	NAD+ binding
C	0017136	molecular_function	NAD-dependent histone deacetylase activity
C	0051287	molecular_function	NAD binding
C	0070403	molecular_function	NAD+ binding
D	0017136	molecular_function	NAD-dependent histone deacetylase activity
D	0051287	molecular_function	NAD binding
D	0070403	molecular_function	NAD+ binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue ZN A 501

Chain	Residue
A	CYS195
A	CYS200
A	CYS221
A	CYS224

---

site_id	AC2
Number of Residues	27
Details	binding site for residue OMR A 502

Chain	Residue
A	PHE96
A	ARG97
A	TYR104
A	PHE119
A	PHE143
A	GLN167
A	ILE169
A	PHE235
A	GLY261
A	THR262
A	SER263
A	VAL266
A	ASN286
A	LYS287
A	GLU288
A	GLY322
A	GLU323
A	CYS324
A	HOH601
A	HOH614
A	HOH625
D	SER238
A	GLY84
A	ALA85
A	GLY86
A	THR89
A	ASP95

---

site_id	AC3
Number of Residues	4
Details	binding site for residue ZN B 501

Chain	Residue
B	CYS195
B	CYS200
B	CYS221
B	CYS224

---

site_id	AC4
Number of Residues	27
Details	binding site for residue OMR B 502

Chain	Residue
B	GLY84
B	ALA85
B	GLY86
B	THR89
B	ASP95
B	PHE96
B	ARG97
B	TYR104
B	PHE119
B	LEU138
B	GLN167
B	HIS187
B	PHE235
B	GLY261
B	THR262
B	SER263
B	VAL266
B	ASN286
B	LYS287
B	GLU288
B	GLY322
B	GLU323
B	CYS324
B	HOH603
B	HOH614
B	HOH624
B	HOH627

---

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN C 501

Chain	Residue
C	CYS195
C	CYS200
C	CYS221
C	CYS224

---

site_id	AC6
Number of Residues	27
Details	binding site for residue OMR C 502

Chain	Residue
C	GLY84
C	ALA85
C	GLY86
C	THR89
C	ASP95
C	PHE96
C	ARG97
C	TYR104
C	PHE119
C	GLN167
C	HIS187
C	PHE190
C	PHE235
C	GLY261
C	THR262
C	SER263
C	VAL266
C	ASN286
C	LYS287
C	GLU288
C	GLY322
C	GLU323
C	CYS324
C	HOH604
C	HOH605
C	HOH611
C	HOH636

---

site_id	AC7
Number of Residues	4
Details	binding site for residue ZN D 501

Chain	Residue
D	CYS195
D	CYS200
D	CYS221
D	CYS224

---

site_id	AC8
Number of Residues	20
Details	binding site for residue OMR D 502

Chain	Residue
D	GLY86
D	THR89
D	ASP95
D	ARG97
D	PHE119
D	LEU138
D	HIS187
D	PHE190
D	GLY261
D	THR262
D	SER263
D	VAL266
D	ASN286
D	LYS287
D	GLU288
D	GLY322
D	GLU323
D	CYS324
D	GLY84
D	ALA85

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00236

Chain	Residue	Details
A	HIS187
B	HIS187
C	HIS187
D	HIS187

---

site_id	SWS_FT_FI2
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269|PubMed:25672491, ECO:0007744|PDB:4RMG

Chain	Residue	Details
A	ALA85
B	THR262
B	ASN286
B	GLY336
C	ALA85
C	ASP95
C	GLN167
C	THR262
C	ASN286
C	GLY336
D	ALA85
A	ASP95
D	ASP95
D	GLN167
D	THR262
D	ASN286
D	GLY336
A	GLN167
A	THR262
A	ASN286
A	GLY336
B	ALA85
B	ASP95
B	GLN167

---

site_id	SWS_FT_FI3
Number of Residues	16
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
C	CYS200
C	CYS221
C	CYS224
D	CYS195
D	CYS200
D	CYS221
D	CYS224
A	CYS200
A	CYS221
A	CYS224
B	CYS195
B	CYS200
B	CYS221
B	CYS224
C	CYS195

---

site_id	SWS_FT_FI4
Number of Residues	12
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5RJQ4

Chain	Residue	Details
A	SER53
D	SER53
D	SER100
D	SER207
A	SER100
A	SER207
B	SER53
B	SER100
B	SER207
C	SER53
C	SER100
C	SER207

---