4IXZ

Native structure of cystathionine gamma lyase (XometC) from xanthomonas oryzae pv. oryzae at pH 9.0

Replaces:  3NMY

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000096	biological_process	sulfur amino acid metabolic process
A	0003962	molecular_function	cystathionine gamma-synthase activity
A	0004123	molecular_function	cystathionine gamma-lyase activity
A	0005737	cellular_component	cytoplasm
A	0016846	molecular_function	carbon-sulfur lyase activity
A	0019343	biological_process	cysteine biosynthetic process via cystathionine
A	0019346	biological_process	transsulfuration
A	0030170	molecular_function	pyridoxal phosphate binding
B	0000096	biological_process	sulfur amino acid metabolic process
B	0003962	molecular_function	cystathionine gamma-synthase activity
B	0004123	molecular_function	cystathionine gamma-lyase activity
B	0005737	cellular_component	cytoplasm
B	0016846	molecular_function	carbon-sulfur lyase activity
B	0019343	biological_process	cysteine biosynthetic process via cystathionine
B	0019346	biological_process	transsulfuration
B	0030170	molecular_function	pyridoxal phosphate binding
C	0000096	biological_process	sulfur amino acid metabolic process
C	0003962	molecular_function	cystathionine gamma-synthase activity
C	0004123	molecular_function	cystathionine gamma-lyase activity
C	0005737	cellular_component	cytoplasm
C	0016846	molecular_function	carbon-sulfur lyase activity
C	0019343	biological_process	cysteine biosynthetic process via cystathionine
C	0019346	biological_process	transsulfuration
C	0030170	molecular_function	pyridoxal phosphate binding
D	0000096	biological_process	sulfur amino acid metabolic process
D	0003962	molecular_function	cystathionine gamma-synthase activity
D	0004123	molecular_function	cystathionine gamma-lyase activity
D	0005737	cellular_component	cytoplasm
D	0016846	molecular_function	carbon-sulfur lyase activity
D	0019343	biological_process	cysteine biosynthetic process via cystathionine
D	0019346	biological_process	transsulfuration
D	0030170	molecular_function	pyridoxal phosphate binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE BCT A 401

Chain	Residue
A	TYR112
A	ASN160
A	LLP210
A	SER339
A	LEU340
A	THR354
A	ARG374
A	HOH680

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME A 402

Chain	Residue
A	ARG266
A	CYS269
A	GLY308
A	HOH553
A	LEU193

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site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BME B 401

Chain	Residue
B	LEU193
B	MET265
B	ARG266
B	CYS269
B	GLY308
B	PHE309
B	HOH596

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site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME C 401

Chain	Residue
C	LEU193
C	ARG266
C	CYS269
C	GLY308
C	HOH678

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site_id	AC5
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL D 401

Chain	Residue
A	ASP167
A	ILE168
A	ALA169
A	ARG304
A	GLN305
D	ALA294
D	SER295
D	HIS296
D	PRO297

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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. DLvvhSATKYLnGHS

Chain	Residue	Details
A	ASP202-SER216

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