7F1U

Crystal structure of Pseudomonas putida methionine gamma-lyase Q349S mutant with L-methionine intermediates

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0016829	molecular_function	lyase activity
A	0016846	molecular_function	carbon-sulfur lyase activity
A	0018826	molecular_function	methionine gamma-lyase activity
A	0019346	biological_process	transsulfuration
A	0030170	molecular_function	pyridoxal phosphate binding
A	0047982	molecular_function	homocysteine desulfhydrase activity
B	0005737	cellular_component	cytoplasm
B	0016829	molecular_function	lyase activity
B	0016846	molecular_function	carbon-sulfur lyase activity
B	0018826	molecular_function	methionine gamma-lyase activity
B	0019346	biological_process	transsulfuration
B	0030170	molecular_function	pyridoxal phosphate binding
B	0047982	molecular_function	homocysteine desulfhydrase activity
C	0005737	cellular_component	cytoplasm
C	0016829	molecular_function	lyase activity
C	0016846	molecular_function	carbon-sulfur lyase activity
C	0018826	molecular_function	methionine gamma-lyase activity
C	0019346	biological_process	transsulfuration
C	0030170	molecular_function	pyridoxal phosphate binding
C	0047982	molecular_function	homocysteine desulfhydrase activity
D	0005737	cellular_component	cytoplasm
D	0016829	molecular_function	lyase activity
D	0016846	molecular_function	carbon-sulfur lyase activity
D	0018826	molecular_function	methionine gamma-lyase activity
D	0019346	biological_process	transsulfuration
D	0030170	molecular_function	pyridoxal phosphate binding
D	0047982	molecular_function	homocysteine desulfhydrase activity

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. DLvvhSATKYLsGHG

Chain	Residue	Details
B	ASP203-GLY217
A	ASP203-GLY217

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|Ref.7

Chain	Residue	Details
B	TYR59
C	TYR59
D	TYR59

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: in other chain => ECO:0000269|Ref.7

Chain	Residue	Details
B	GLY89
B	SER208
C	GLY89
C	SER208
D	GLY89
D	SER208

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:22785484, ECO:0007744|PDB:3VK3, ECO:0007744|PDB:3VK4

Chain	Residue	Details
B	TYR114
B	ARG375
C	TYR114
C	ARG375
D	TYR114
D	ARG375

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:17289792, ECO:0000269|PubMed:22785484, ECO:0000269|PubMed:3365412, ECO:0000269|Ref.7, ECO:0000269|Ref.8, ECO:0007744|PDB:1UKJ

Chain	Residue	Details
B	LLP211
C	LYS211
D	LYS211

---