3C6K

Crystal structure of human spermine synthase in complex with spermidine and 5-methylthioadenosine

Replaces:  2QFM

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005829	cellular_component	cytosol
A	0006555	biological_process	methionine metabolic process
A	0006595	biological_process	polyamine metabolic process
A	0006596	biological_process	polyamine biosynthetic process
A	0006597	biological_process	spermine biosynthetic process
A	0008215	biological_process	spermine metabolic process
A	0016740	molecular_function	transferase activity
A	0016768	molecular_function	spermine synthase activity
A	0070062	cellular_component	extracellular exosome
B	0005829	cellular_component	cytosol
B	0006555	biological_process	methionine metabolic process
B	0006595	biological_process	polyamine metabolic process
B	0006596	biological_process	polyamine biosynthetic process
B	0006597	biological_process	spermine biosynthetic process
B	0008215	biological_process	spermine metabolic process
B	0016740	molecular_function	transferase activity
B	0016768	molecular_function	spermine synthase activity
B	0070062	cellular_component	extracellular exosome
C	0005829	cellular_component	cytosol
C	0006555	biological_process	methionine metabolic process
C	0006595	biological_process	polyamine metabolic process
C	0006596	biological_process	polyamine biosynthetic process
C	0006597	biological_process	spermine biosynthetic process
C	0008215	biological_process	spermine metabolic process
C	0016740	molecular_function	transferase activity
C	0016768	molecular_function	spermine synthase activity
C	0070062	cellular_component	extracellular exosome
D	0005829	cellular_component	cytosol
D	0006555	biological_process	methionine metabolic process
D	0006595	biological_process	polyamine metabolic process
D	0006596	biological_process	polyamine biosynthetic process
D	0006597	biological_process	spermine biosynthetic process
D	0008215	biological_process	spermine metabolic process
D	0016740	molecular_function	transferase activity
D	0016768	molecular_function	spermine synthase activity
D	0070062	cellular_component	extracellular exosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SPD A 501

Chain	Residue
A	ASP169
A	HOH537
A	HOH574
A	VAL170
A	ASN171
A	TYR179
A	ASP278
A	LEU279
A	TYR353
A	GLU355
A	TRP357

---

site_id	AC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SPD B 501

Chain	Residue
B	ASP169
B	VAL170
B	ASN171
B	TYR179
B	ASP278
B	LEU279
B	TYR353
B	GLU355
B	TRP357
B	HOH522
B	HOH530

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE SPD C 501

Chain	Residue
C	ASP169
C	VAL170
C	ASN171
C	TYR179
C	ASP278
C	LEU279
C	TYR353
C	GLU355
C	TRP357
C	HOH752
C	HOH778

---

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE SPD D 501

Chain	Residue
D	ASP169
D	VAL170
D	ASN171
D	TYR179
D	ASP278
D	LEU279
D	TYR353
D	GLU355
D	TRP357
D	HOH687
D	HOH689
D	HOH692

---

site_id	AC5
Number of Residues	18
Details	BINDING SITE FOR RESIDUE MTA A 401

Chain	Residue
A	GLN150
A	LEU164
A	LEU166
A	ASN171
A	GLY200
A	GLY202
A	ASP203
A	VAL221
A	GLU222
A	ILE223
A	ASP224
A	VAL227
A	ASP257
A	CYS258
A	ASP278
A	LEU279
A	THR280
A	ILE284

---

site_id	AC6
Number of Residues	18
Details	BINDING SITE FOR RESIDUE MTA B 401

Chain	Residue
B	GLN150
B	LEU164
B	LEU166
B	GLY200
B	GLY201
B	GLY202
B	ASP203
B	VAL221
B	GLU222
B	ILE223
B	ASP224
B	VAL227
B	ASP257
B	CYS258
B	ASP278
B	LEU279
B	THR280
B	ILE284

---

site_id	AC7
Number of Residues	15
Details	BINDING SITE FOR RESIDUE MTA C 401

Chain	Residue
C	GLN150
C	LEU164
C	LEU166
C	GLY200
C	VAL221
C	GLU222
C	ILE223
C	ASP224
C	VAL227
C	ASP257
C	CYS258
C	ASP278
C	LEU279
C	THR280
C	ILE284

---

site_id	AC8
Number of Residues	16
Details	BINDING SITE FOR RESIDUE MTA D 401

Chain	Residue
D	ASN171
D	GLY200
D	GLY202
D	VAL221
D	GLU222
D	ILE223
D	VAL227
D	ASP257
D	CYS258
D	ASP278
D	LEU279
D	THR280
D	ILE284
D	GLN150
D	LEU164
D	LEU166

---

Functional Information from PROSITE/UniProt

site_id	PS01330
Number of Residues	14
Details	PABS_1 Polyamine biosynthesis (PABS) domain signature. VLILGGGdGgiLcE

Chain	Residue	Details
A	VAL196-GLU209

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00354, ECO:0000269|PubMed:18367445

Chain	Residue	Details
A	ASP278
B	ASP278
C	ASP278
D	ASP278

---

site_id	SWS_FT_FI2
Number of Residues	28
Details	BINDING: BINDING => ECO:0000269|PubMed:18367445

Chain	Residue	Details
A	GLN150
B	ASP203
B	GLU222
B	ASP257
B	TYR353
B	GLU355
C	GLN150
C	TYR179
C	ASP203
C	GLU222
C	ASP257
A	TYR179
C	TYR353
C	GLU355
D	GLN150
D	TYR179
D	ASP203
D	GLU222
D	ASP257
D	TYR353
D	GLU355
A	ASP203
A	GLU222
A	ASP257
A	TYR353
A	GLU355
B	GLN150
B	TYR179

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER59
B	SER59
C	SER59
D	SER59

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