Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6E1X

Crystal structure of product-bound complex of spermidine/spermine N-acetyltransferase SpeG

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0004145	molecular_function	diamine N-acetyltransferase activity
A	0005737	cellular_component	cytoplasm
A	0006598	biological_process	polyamine catabolic process
A	0016740	molecular_function	transferase activity
A	0016746	molecular_function	acyltransferase activity
A	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
A	0046203	biological_process	spermidine catabolic process
A	0046208	biological_process	spermine catabolic process
A	0046872	molecular_function	metal ion binding
B	0000287	molecular_function	magnesium ion binding
B	0004145	molecular_function	diamine N-acetyltransferase activity
B	0005737	cellular_component	cytoplasm
B	0006598	biological_process	polyamine catabolic process
B	0016740	molecular_function	transferase activity
B	0016746	molecular_function	acyltransferase activity
B	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
B	0046203	biological_process	spermidine catabolic process
B	0046208	biological_process	spermine catabolic process
B	0046872	molecular_function	metal ion binding
C	0000287	molecular_function	magnesium ion binding
C	0004145	molecular_function	diamine N-acetyltransferase activity
C	0005737	cellular_component	cytoplasm
C	0006598	biological_process	polyamine catabolic process
C	0016740	molecular_function	transferase activity
C	0016746	molecular_function	acyltransferase activity
C	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
C	0046203	biological_process	spermidine catabolic process
C	0046208	biological_process	spermine catabolic process
C	0046872	molecular_function	metal ion binding
D	0000287	molecular_function	magnesium ion binding
D	0004145	molecular_function	diamine N-acetyltransferase activity
D	0005737	cellular_component	cytoplasm
D	0006598	biological_process	polyamine catabolic process
D	0016740	molecular_function	transferase activity
D	0016746	molecular_function	acyltransferase activity
D	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
D	0046203	biological_process	spermidine catabolic process
D	0046208	biological_process	spermine catabolic process
D	0046872	molecular_function	metal ion binding
E	0000287	molecular_function	magnesium ion binding
E	0004145	molecular_function	diamine N-acetyltransferase activity
E	0005737	cellular_component	cytoplasm
E	0006598	biological_process	polyamine catabolic process
E	0016740	molecular_function	transferase activity
E	0016746	molecular_function	acyltransferase activity
E	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
E	0046203	biological_process	spermidine catabolic process
E	0046208	biological_process	spermine catabolic process
E	0046872	molecular_function	metal ion binding
F	0000287	molecular_function	magnesium ion binding
F	0004145	molecular_function	diamine N-acetyltransferase activity
F	0005737	cellular_component	cytoplasm
F	0006598	biological_process	polyamine catabolic process
F	0016740	molecular_function	transferase activity
F	0016746	molecular_function	acyltransferase activity
F	0016747	molecular_function	acyltransferase activity, transferring groups other than amino-acyl groups
F	0046203	biological_process	spermidine catabolic process
F	0046208	biological_process	spermine catabolic process
F	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	binding site for residue SPM A 201

Chain	Residue
A	ASN22
A	HOH383
A	HOH405
E	HIS49
E	ILE50
E	ASP52
E	GLU55
A	MET28
A	GLU33
A	TYR36
A	GLU41
A	HOH305
A	HOH312
A	HOH342
A	HOH361

site_id	AC2
Number of Residues	13
Details	binding site for residue SP5 A 202

Chain	Residue
A	TYR30
A	TRP31
A	PHE85
A	GLN86
A	ILE87
A	HIS122
A	TYR134
A	GLU148
A	PHE149
A	HOH303
A	HOH379
A	HOH398
A	HOH478

site_id	AC3
Number of Residues	4
Details	binding site for residue MRD A 203

Chain	Residue
A	TYR30
A	ILE88
A	ILE89
A	GLN94

site_id	AC4
Number of Residues	7
Details	binding site for residue TRS A 204

Chain	Residue
A	ASN53
A	ARG56
A	ILE76
A	TYR78
A	HOH307
A	HOH434
D	TYR78

site_id	AC5
Number of Residues	15
Details	binding site for residue SPM B 201

Chain	Residue
B	ASN22
B	MET28
B	GLU33
B	TYR36
B	GLU41
B	HOH305
B	HOH312
B	HOH344
B	HOH363
B	HOH399
F	HIS49
F	ILE50
F	ASP52
F	GLU55
F	HOH204

site_id	AC6
Number of Residues	19
Details	binding site for residue SP5 B 202

Chain	Residue
B	TYR30
B	TRP31
B	GLU75
B	GLU84
B	PHE85
B	GLN86
B	ILE87
B	HIS122
B	TYR134
B	GLU148
B	PHE149
B	HOH307
B	HOH316
B	HOH360
B	HOH374
B	HOH376
B	HOH449
B	HOH539
F	HOH409

site_id	AC7
Number of Residues	4
Details	binding site for residue MPD B 203

Chain	Residue
B	TYR30
B	ILE88
B	ILE89
B	GLN94

site_id	AC8
Number of Residues	8
Details	binding site for residue TRS B 204

Chain	Residue
B	ASN53
B	ARG56
B	ILE76
B	TYR78
B	HOH306
B	HOH361
B	HOH404
C	TYR78

site_id	AC9
Number of Residues	15
Details	binding site for residue SPM C 201

Chain	Residue
C	HOH395
B	HIS49
B	ILE50
B	ASP52
B	GLU55
B	HOH311
C	ASN22
C	MET28
C	GLU33
C	TYR36
C	GLU41
C	HOH301
C	HOH313
C	HOH326
C	HOH327

site_id	AD1
Number of Residues	10
Details	binding site for residue SPM C 202

Chain	Residue
B	TYR78
C	HIS49
C	ILE50
C	ASP52
C	GLU55
C	HOH304
C	HOH337
C	HOH467
F	GLU34
F	GLU41

site_id	AD2
Number of Residues	10
Details	binding site for residue HLG C 203

Chain	Residue
C	TYR30
C	TRP31
C	PHE85
C	GLN86
C	ILE87
C	HIS122
C	TYR134
C	HOH367
C	HOH373
C	HOH417

site_id	AD3
Number of Residues	5
Details	binding site for residue MRD C 204

Chain	Residue
C	LYS129
C	TYR134
C	MRD205
C	HOH343
E	HOH327

site_id	AD4
Number of Residues	7
Details	binding site for residue MRD C 205

Chain	Residue
C	ILE87
C	ILE88
C	ILE89
C	GLN94
C	MRD204
C	HOH397
E	ASN170

site_id	AD5
Number of Residues	1
Details	binding site for residue MPD C 206

Chain	Residue
C	LYS48

site_id	AD6
Number of Residues	15
Details	binding site for residue SPM D 201

Chain	Residue
A	HIS49
A	ILE50
A	ASP52
A	GLU55
A	HOH314
D	ASN22
D	MET28
D	GLU33
D	GLU34
D	TYR36
D	GLU41
D	HOH301
D	HOH314
D	HOH319
D	HOH325

site_id	AD7
Number of Residues	12
Details	binding site for residue SP5 D 202

Chain	Residue
D	TYR30
D	TRP31
D	GLU75
D	PHE85
D	GLN86
D	ILE87
D	HIS122
D	TYR134
D	HOH352
D	HOH359
D	HOH406
D	HOH461

site_id	AD8
Number of Residues	4
Details	binding site for residue MRD D 203

Chain	Residue
D	LYS129
D	TYR134
D	HOH308
F	HOH227

site_id	AD9
Number of Residues	7
Details	binding site for residue MRD D 204

Chain	Residue
D	TYR30
D	ILE87
D	ILE88
D	ILE89
D	GLN94
D	HOH414
F	ASN170

site_id	AE1
Number of Residues	1
Details	binding site for residue MPD D 205

Chain	Residue
D	LYS48

site_id	AE2
Number of Residues	11
Details	binding site for residue SPM E 201

Chain	Residue
A	TYR78
D	HIS49
D	ILE50
D	ASP52
D	GLU55
D	HOH335
E	GLU34
E	GLU37
E	GLU41
E	HOH308
E	HOH454

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	942
Details	Domain: {"description":"N-acetyltransferase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00532","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	6
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P0A951","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2013","submissionDatabase":"PDB data bank","title":"Crystal structure of spermidine N-acetyltransferase from Vibrio cholerae in complex with polyamine.","authors":["Filippova E.V.","Minasov G.","Shuvalova L.","Kiryukhina O.","Kuhn M.L.","Anderson W.F."]}},{"source":"PDB","id":"4MJ8","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MI4","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MI4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4R87","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	18
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R87","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26410587","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5CNP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R57","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4R87","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	54
Details	Binding site: {"evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4R57","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	6
Details	Site: {"description":"Could be important for selectivity toward long polyamines","evidences":[{"source":"PubMed","id":"25623305","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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