Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1QGN

CYSTATHIONINE GAMMA-SYNTHASE FROM NICOTIANA TABACUM

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003962	molecular_function	cystathionine gamma-synthase activity
A	0009086	biological_process	methionine biosynthetic process
A	0019346	biological_process	transsulfuration
A	0030170	molecular_function	pyridoxal phosphate binding
B	0003962	molecular_function	cystathionine gamma-synthase activity
B	0009086	biological_process	methionine biosynthetic process
B	0019346	biological_process	transsulfuration
B	0030170	molecular_function	pyridoxal phosphate binding
C	0003962	molecular_function	cystathionine gamma-synthase activity
C	0009086	biological_process	methionine biosynthetic process
C	0019346	biological_process	transsulfuration
C	0030170	molecular_function	pyridoxal phosphate binding
D	0003962	molecular_function	cystathionine gamma-synthase activity
D	0009086	biological_process	methionine biosynthetic process
D	0019346	biological_process	transsulfuration
D	0030170	molecular_function	pyridoxal phosphate binding
E	0003962	molecular_function	cystathionine gamma-synthase activity
E	0009086	biological_process	methionine biosynthetic process
E	0019346	biological_process	transsulfuration
E	0030170	molecular_function	pyridoxal phosphate binding
F	0003962	molecular_function	cystathionine gamma-synthase activity
F	0009086	biological_process	methionine biosynthetic process
F	0019346	biological_process	transsulfuration
F	0030170	molecular_function	pyridoxal phosphate binding
G	0003962	molecular_function	cystathionine gamma-synthase activity
G	0009086	biological_process	methionine biosynthetic process
G	0019346	biological_process	transsulfuration
G	0030170	molecular_function	pyridoxal phosphate binding
H	0003962	molecular_function	cystathionine gamma-synthase activity
H	0009086	biological_process	methionine biosynthetic process
H	0019346	biological_process	transsulfuration
H	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PLP A 500

Chain	Residue
A	SER137
C	TYR108
C	ARG110
A	GLY138
A	MET139
A	TYR163
A	ASP236
A	SER258
A	THR260
A	LYS261
A	PHE389

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP B 500

Chain	Residue
B	SER137
B	GLY138
B	MET139
B	TYR163
B	ASP236
B	THR238
B	SER258
B	THR260
B	LYS261
B	PHE389
D	TYR108
D	ARG110

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PLP C 500

Chain	Residue
A	TYR108
A	ARG110
C	SER137
C	GLY138
C	MET139
C	TYR163
C	ASP236
C	SER258
C	THR260
C	LYS261
C	PHE389

site_id	AC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PLP D 500

Chain	Residue
B	TYR108
B	ARG110
D	SER137
D	GLY138
D	MET139
D	ASP236
D	SER258
D	THR260
D	LYS261
D	PHE389

site_id	AC5
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PLP E 500

Chain	Residue
E	SER137
E	GLY138
E	MET139
E	TYR163
E	ASP236
E	SER258
E	THR260
E	LYS261
E	PHE389
G	TYR108
G	ARG110

site_id	AC6
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP F 500

Chain	Residue
F	SER137
F	GLY138
F	MET139
F	TYR163
F	ASP236
F	THR238
F	SER258
F	THR260
F	LYS261
F	PHE389
H	TYR108
H	ARG110

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP G 500

Chain	Residue
E	TYR108
E	ARG110
G	SER137
G	GLY138
G	MET139
G	TYR163
G	ASP236
G	THR238
G	SER258
G	THR260
G	LYS261
G	PHE389

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PLP H 500

Chain	Residue
F	TYR108
F	ARG110
H	SER137
H	GLY138
H	MET139
H	TYR163
H	ASP236
H	SER258
H	THR260
H	LYS261
H	PHE389

Functional Information from PROSITE/UniProt

site_id	PS00868
Number of Residues	15
Details	CYS_MET_METAB_PP Cys/Met metabolism enzymes pyridoxal-phosphate attachment site. DLvlhSATKFLgGHN

Chain	Residue	Details
A	ASP253-ASN267

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	48
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10438597","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11518531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1I43","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1I48","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QGN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"10438597","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11518531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1I48","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QGN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"10438597","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11518531","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1I43","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1I48","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QGN","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details

Chain	Residue	Details
A	ASP236
A	LYS261
A	TYR163

site_id	CSA2
Number of Residues	3
Details

Chain	Residue	Details
B	ASP236
B	LYS261
B	TYR163

site_id	CSA3
Number of Residues	3
Details

Chain	Residue	Details
C	ASP236
C	LYS261
C	TYR163

site_id	CSA4
Number of Residues	3
Details

Chain	Residue	Details
D	ASP236
D	LYS261
D	TYR163

site_id	CSA5
Number of Residues	3
Details

Chain	Residue	Details
E	ASP236
E	LYS261
E	TYR163

site_id	CSA6
Number of Residues	3
Details

Chain	Residue	Details
F	ASP236
F	LYS261
F	TYR163

site_id	CSA7
Number of Residues	3
Details

Chain	Residue	Details
G	ASP236
G	LYS261
G	TYR163

site_id	CSA8
Number of Residues	3
Details

Chain	Residue	Details
H	ASP236
H	LYS261
H	TYR163

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