Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3COG

Crystal structure of human cystathionase (Cystathionine gamma lyase) in complex with DL-propargylglycine

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004123	molecular_function	cystathionine gamma-lyase activity
A	0005515	molecular_function	protein binding
A	0005516	molecular_function	calmodulin binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006534	biological_process	cysteine metabolic process
A	0006629	biological_process	lipid metabolic process
A	0008652	biological_process	amino acid biosynthetic process
A	0016829	molecular_function	lyase activity
A	0018272	biological_process	protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine
A	0019343	biological_process	cysteine biosynthetic process via cystathionine
A	0019344	biological_process	cysteine biosynthetic process
A	0019346	biological_process	transsulfuration
A	0030170	molecular_function	pyridoxal phosphate binding
A	0030968	biological_process	endoplasmic reticulum unfolded protein response
A	0042802	molecular_function	identical protein binding
A	0043066	biological_process	negative regulation of apoptotic process
A	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
A	0044524	biological_process	protein sulfhydration
A	0044540	molecular_function	L-cystine L-cysteine-lyase (deaminating)
A	0047982	molecular_function	homocysteine desulfhydrase activity
A	0051289	biological_process	protein homotetramerization
A	0070062	cellular_component	extracellular exosome
A	0070814	biological_process	hydrogen sulfide biosynthetic process
A	0080146	molecular_function	L-cysteine desulfhydrase activity
A	0098606	molecular_function	selenocystathionine gamma-lyase activity
A	1904831	biological_process	positive regulation of aortic smooth muscle cell differentiation
B	0004123	molecular_function	cystathionine gamma-lyase activity
B	0005515	molecular_function	protein binding
B	0005516	molecular_function	calmodulin binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006534	biological_process	cysteine metabolic process
B	0006629	biological_process	lipid metabolic process
B	0008652	biological_process	amino acid biosynthetic process
B	0016829	molecular_function	lyase activity
B	0018272	biological_process	protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine
B	0019343	biological_process	cysteine biosynthetic process via cystathionine
B	0019344	biological_process	cysteine biosynthetic process
B	0019346	biological_process	transsulfuration
B	0030170	molecular_function	pyridoxal phosphate binding
B	0030968	biological_process	endoplasmic reticulum unfolded protein response
B	0042802	molecular_function	identical protein binding
B	0043066	biological_process	negative regulation of apoptotic process
B	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
B	0044524	biological_process	protein sulfhydration
B	0044540	molecular_function	L-cystine L-cysteine-lyase (deaminating)
B	0047982	molecular_function	homocysteine desulfhydrase activity
B	0051289	biological_process	protein homotetramerization
B	0070062	cellular_component	extracellular exosome
B	0070814	biological_process	hydrogen sulfide biosynthetic process
B	0080146	molecular_function	L-cysteine desulfhydrase activity
B	0098606	molecular_function	selenocystathionine gamma-lyase activity
B	1904831	biological_process	positive regulation of aortic smooth muscle cell differentiation
C	0004123	molecular_function	cystathionine gamma-lyase activity
C	0005515	molecular_function	protein binding
C	0005516	molecular_function	calmodulin binding
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006534	biological_process	cysteine metabolic process
C	0006629	biological_process	lipid metabolic process
C	0008652	biological_process	amino acid biosynthetic process
C	0016829	molecular_function	lyase activity
C	0018272	biological_process	protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine
C	0019343	biological_process	cysteine biosynthetic process via cystathionine
C	0019344	biological_process	cysteine biosynthetic process
C	0019346	biological_process	transsulfuration
C	0030170	molecular_function	pyridoxal phosphate binding
C	0030968	biological_process	endoplasmic reticulum unfolded protein response
C	0042802	molecular_function	identical protein binding
C	0043066	biological_process	negative regulation of apoptotic process
C	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
C	0044524	biological_process	protein sulfhydration
C	0044540	molecular_function	L-cystine L-cysteine-lyase (deaminating)
C	0047982	molecular_function	homocysteine desulfhydrase activity
C	0051289	biological_process	protein homotetramerization
C	0070062	cellular_component	extracellular exosome
C	0070814	biological_process	hydrogen sulfide biosynthetic process
C	0080146	molecular_function	L-cysteine desulfhydrase activity
C	0098606	molecular_function	selenocystathionine gamma-lyase activity
C	1904831	biological_process	positive regulation of aortic smooth muscle cell differentiation
D	0004123	molecular_function	cystathionine gamma-lyase activity
D	0005515	molecular_function	protein binding
D	0005516	molecular_function	calmodulin binding
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006534	biological_process	cysteine metabolic process
D	0006629	biological_process	lipid metabolic process
D	0008652	biological_process	amino acid biosynthetic process
D	0016829	molecular_function	lyase activity
D	0018272	biological_process	protein-pyridoxal-5-phosphate linkage via peptidyl-N6-pyridoxal phosphate-L-lysine
D	0019343	biological_process	cysteine biosynthetic process via cystathionine
D	0019344	biological_process	cysteine biosynthetic process
D	0019346	biological_process	transsulfuration
D	0030170	molecular_function	pyridoxal phosphate binding
D	0030968	biological_process	endoplasmic reticulum unfolded protein response
D	0042802	molecular_function	identical protein binding
D	0043066	biological_process	negative regulation of apoptotic process
D	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
D	0044524	biological_process	protein sulfhydration
D	0044540	molecular_function	L-cystine L-cysteine-lyase (deaminating)
D	0047982	molecular_function	homocysteine desulfhydrase activity
D	0051289	biological_process	protein homotetramerization
D	0070062	cellular_component	extracellular exosome
D	0070814	biological_process	hydrogen sulfide biosynthetic process
D	0080146	molecular_function	L-cysteine desulfhydrase activity
D	0098606	molecular_function	selenocystathionine gamma-lyase activity
D	1904831	biological_process	positive regulation of aortic smooth muscle cell differentiation

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NO3 C 606

Chain	Residue
C	TYR114
C	ASN161
C	LYS212
C	SER340
C	LEU341
C	THR355
C	ARG375

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NO3 D 607

Chain	Residue
D	LYS212
D	SER340
D	LEU341
D	THR355
D	ARG375
D	TYR114
D	ASN161

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE NO3 A 608

Chain	Residue
A	TYR114
A	ASN161
A	LYS212
A	SER340
A	LEU341
A	THR355
A	ARG375

site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP A 500

Chain	Residue
A	SER89
A	GLY90
A	LEU91
A	TYR114
A	ASN161
A	ASP187
A	THR189
A	SER209
A	THR211
A	LYS212
B	TYR60
B	ARG62

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PLP C 500

Chain	Residue
C	SER89
C	GLY90
C	LEU91
C	TYR114
C	ASN161
C	ASP187
C	THR189
C	SER209
C	THR211
C	LYS212
D	TYR60
D	ARG62

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

Chain	Residue
C	TYR60
C	ARG62
D	SER89
D	GLY90
D	LEU91
D	TYR114
D	ASN161
D	ASP187
D	SER209
D	THR211
D	LYS212
D	LEU341

site_id	AC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 2AG A 501

Chain	Residue
A	TYR114
A	ARG119
A	GLU339
B	TYR60
B	ARG62

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE 2AG C 501

Chain	Residue
C	TYR114
C	ARG119
C	GLU339
D	TYR60
D	ARG62

site_id	AC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE 2AG D 501

Chain	Residue
C	GLU59
C	TYR60
C	ARG62
D	TYR114
D	ARG119
D	GLU339

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL D 601

Chain	Residue
C	GLU127
D	HIS99
D	LEU100
D	LEU101

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 602

Chain	Residue
C	HIS99
C	LEU100
C	LEU101
D	GLU127

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 603

Chain	Residue
A	HIS99
A	LEU100
A	LEU101
B	GLU127

site_id	BC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 604

Chain	Residue
B	TRP32
B	THR33
B	SER34
D	TRP32
D	THR33
D	SER34

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 605

Chain	Residue
C	LEU43
C	SER248
C	PRO249
D	ASP219
D	ASP251

site_id	BC6
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PEG A 609

Chain	Residue
A	GLN299
A	HIS300
A	GLU301
A	LEU302
A	ARG305
A	PRO295
A	HIS297
A	PRO298

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. DIsmySATKYMnGHS

Chain	Residue	Details
A	ASP204-SER218

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	15
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"19019829","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	ASP187
A	TYR114

site_id	CSA10
Number of Residues	1
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
C	ARG62

site_id	CSA11
Number of Residues	1
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
D	ARG62

site_id	CSA12
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	LYS212
A	SER209
A	GLN49

site_id	CSA13
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
B	LYS212
B	SER209
B	GLN49

site_id	CSA14
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
C	LYS212
C	SER209
C	GLN49

site_id	CSA15
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
D	LYS212
D	SER209
D	GLN49

site_id	CSA16
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	LYS212
A	ASP187
A	PHE121

site_id	CSA17
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
B	LYS212
B	ASP187
B	PHE121

site_id	CSA18
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
C	LYS212
C	ASP187
C	PHE121

site_id	CSA19
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
D	LYS212
D	ASP187
D	PHE121

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
B	ASP187
B	TYR114

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
C	ASP187
C	TYR114

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
D	ASP187
D	TYR114

site_id	CSA5
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
A	LYS212
A	ASP187
A	TYR114

site_id	CSA6
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
B	LYS212
B	ASP187
B	TYR114

site_id	CSA7
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
C	LYS212
C	ASP187
C	TYR114

site_id	CSA8
Number of Residues	3
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
D	LYS212
D	ASP187
D	TYR114

site_id	CSA9
Number of Residues	1
Details	Annotated By Reference To The Literature 1b8g

Chain	Residue	Details
B	ARG62

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