1IBJ

Crystal structure of cystathionine beta-lyase from Arabidopsis thaliana

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004121	molecular_function	obsolete cystathionine beta-lyase activity
A	0006555	biological_process	methionine metabolic process
A	0009086	biological_process	methionine biosynthetic process
A	0009507	cellular_component	chloroplast
A	0009570	cellular_component	chloroplast stroma
A	0016829	molecular_function	lyase activity
A	0019279	biological_process	L-methionine biosynthetic process from L-homoserine via cystathionine
A	0019346	biological_process	transsulfuration
A	0030170	molecular_function	pyridoxal phosphate binding
A	0042803	molecular_function	protein homodimerization activity
A	0047804	molecular_function	cysteine-S-conjugate beta-lyase activity
A	0060090	molecular_function	molecular adaptor activity
A	0071266	biological_process	'de novo' L-methionine biosynthetic process
C	0004121	molecular_function	obsolete cystathionine beta-lyase activity
C	0006555	biological_process	methionine metabolic process
C	0009086	biological_process	methionine biosynthetic process
C	0009507	cellular_component	chloroplast
C	0009570	cellular_component	chloroplast stroma
C	0016829	molecular_function	lyase activity
C	0019279	biological_process	L-methionine biosynthetic process from L-homoserine via cystathionine
C	0019346	biological_process	transsulfuration
C	0030170	molecular_function	pyridoxal phosphate binding
C	0042803	molecular_function	protein homodimerization activity
C	0047804	molecular_function	cysteine-S-conjugate beta-lyase activity
C	0060090	molecular_function	molecular adaptor activity
C	0071266	biological_process	'de novo' L-methionine biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CO3 A 1401

Chain	Residue
A	TYR181
A	SER405
A	ARG440
A	PLP1400

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CO3 C 2401

Chain	Residue
C	HOH2463
C	LYS278
C	SER405
C	PHE406
C	ARG440
C	PLP2400

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 A 500

Chain	Residue
A	GLY365
A	HIS366
A	HIS367
A	LEU368
C	HIS363
C	PRO364
C	GLY365
C	HIS366
C	HIS367
C	LEU368

---

site_id	AC4
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP A 1400

Chain	Residue
A	SER156
A	GLY157
A	MET158
A	TYR181
A	GLU224
A	ASP253
A	SER275
A	THR277
A	LYS278
A	MET287
A	PHE406
A	CO31401
A	HOH1522
C	TYR127
C	ARG129

---

site_id	AC5
Number of Residues	15
Details	BINDING SITE FOR RESIDUE PLP C 2400

Chain	Residue
A	TYR127
A	ARG129
C	GLY157
C	MET158
C	TYR181
C	GLU224
C	ASP253
C	SER275
C	THR277
C	LYS278
C	MET287
C	ALA288
C	PHE406
C	CO32401
C	HOH2463

---

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. DIvmhSATKFIaGHS

Chain	Residue	Details
A	ASP270-SER284

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	BINDING: BINDING => ECO:0000269|PubMed:11402193, ECO:0007744|PDB:1IBJ

Chain	Residue	Details
A	TYR127
C	MET158
C	SER275
C	THR277
A	ARG129
A	GLY157
A	MET158
A	SER275
A	THR277
C	TYR127
C	ARG129
C	GLY157

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11402193, ECO:0007744|PDB:1IBJ

Chain	Residue	Details
A	LYS278
C	LYS278

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	TYR181
A	LYS278
A	ASP253

---

site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
C	TYR181
C	LYS278
C	ASP253

---

site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	ARG129
C	TYR181
C	ASP253

---

site_id	CSA4
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	TYR181
A	ASP253
C	ARG129

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