5V1X

Carbon Sulfoxide lyase, Egt2 Y134F in complex with its substrate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0016829	molecular_function	lyase activity
A	0052699	biological_process	ergothioneine biosynthetic process
A	1990411	molecular_function	hercynylcysteine sulfoxide lyase activity (ergothioneine-forming)
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0016829	molecular_function	lyase activity
B	0052699	biological_process	ergothioneine biosynthetic process
B	1990411	molecular_function	hercynylcysteine sulfoxide lyase activity (ergothioneine-forming)
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0016829	molecular_function	lyase activity
C	0052699	biological_process	ergothioneine biosynthetic process
C	1990411	molecular_function	hercynylcysteine sulfoxide lyase activity (ergothioneine-forming)
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0016829	molecular_function	lyase activity
D	0052699	biological_process	ergothioneine biosynthetic process
D	1990411	molecular_function	hercynylcysteine sulfoxide lyase activity (ergothioneine-forming)
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0016829	molecular_function	lyase activity
E	0052699	biological_process	ergothioneine biosynthetic process
E	1990411	molecular_function	hercynylcysteine sulfoxide lyase activity (ergothioneine-forming)
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0016829	molecular_function	lyase activity
F	0052699	biological_process	ergothioneine biosynthetic process
F	1990411	molecular_function	hercynylcysteine sulfoxide lyase activity (ergothioneine-forming)
G	0005634	cellular_component	nucleus
G	0005737	cellular_component	cytoplasm
G	0016829	molecular_function	lyase activity
G	0052699	biological_process	ergothioneine biosynthetic process
G	1990411	molecular_function	hercynylcysteine sulfoxide lyase activity (ergothioneine-forming)
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0016829	molecular_function	lyase activity
H	0052699	biological_process	ergothioneine biosynthetic process
H	1990411	molecular_function	hercynylcysteine sulfoxide lyase activity (ergothioneine-forming)

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue FMT F 501

Chain	Residue
F	SER47
F	SER196
F	GLN224
F	ARG438

---

site_id	AC2
Number of Residues	6
Details	binding site for residue FMT D 501

Chain	Residue
D	ARG438
D	SER47
D	PHE134
D	SER196
D	GLN224
D	LLP247

---

site_id	AC3
Number of Residues	8
Details	binding site for residue 8VV C 501

Chain	Residue
C	SER47
C	PHE134
C	SER196
C	GLN224
C	LLP247
C	ARG438
D	ARG75
D	PHE304

---

site_id	AC4
Number of Residues	10
Details	binding site for residue 8VV A 501

Chain	Residue
A	GLY46
A	SER47
A	PHE134
A	SER196
A	GLN224
A	LLP247
A	ARG438
B	ARG75
B	HIS276
B	PHE304

---

site_id	AC5
Number of Residues	5
Details	binding site for residue FMT B 501

Chain	Residue
B	SER47
B	SER196
B	GLN224
B	LLP247
B	ARG438

---

site_id	AC6
Number of Residues	1
Details	binding site for residue FMT G 501

Chain	Residue
G	ARG86

---

site_id	AC7
Number of Residues	5
Details	binding site for residue FMT H 501

Chain	Residue
H	SER47
H	SER196
H	GLN224
H	LLP247
H	ARG438

---

site_id	AC8
Number of Residues	14
Details	binding site for Di-peptide ARG B 41 and ASP B 449

Chain	Residue
B	ASN28
B	TYR40
B	ASN42
B	LEU43
B	ASN423
B	THR424
B	LEU445
B	GLU446
B	MET447
B	SER448
B	PHE450
B	GLU451
B	TRP452
B	ALA453

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	16
Details	BINDING: BINDING => ECO:0000269|PubMed:29503207, ECO:0007744|PDB:5V1X

Chain	Residue	Details
E	SER47
A	ARG438
B	SER47
B	ARG438
G	SER47
G	ARG438
H	SER47
H	ARG438
E	ARG438
F	SER47
F	ARG438
D	SER47
D	ARG438
C	SER47
C	ARG438
A	SER47

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:29503207

Chain	Residue	Details
E	LLP247
F	LLP247
D	LLP247
C	LLP247
A	LLP247
B	LLP247
G	LLP247
H	LLP247

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