5V1X

Carbon Sulfoxide lyase, Egt2 Y134F in complex with its substrate

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth E]	UNK_F_TYPE	e5v1xE2	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: UNK_F_TYPE	ECOD (1.6)
A [auth E]	Aminotran_5_N	e5v1xE1	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
D [auth C]	UNK_F_TYPE	e5v1xC2	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: UNK_F_TYPE	ECOD (1.6)
D [auth C]	Aminotran_5_N	e5v1xC1	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
E [auth A]	UNK_F_TYPE	e5v1xA1	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: UNK_F_TYPE	ECOD (1.6)
E [auth A]	Aminotran_5_N	e5v1xA2	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
F [auth B]	UNK_F_TYPE	e5v1xB1	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: UNK_F_TYPE	ECOD (1.6)
F [auth B]	Aminotran_5_N	e5v1xB2	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
B [auth F]	UNK_F_TYPE	e5v1xF2	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: UNK_F_TYPE	ECOD (1.6)
B [auth F]	Aminotran_5_N	e5v1xF1	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
C [auth D]	UNK_F_TYPE	e5v1xD2	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: UNK_F_TYPE	ECOD (1.6)
C [auth D]	Aminotran_5_N	e5v1xD1	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
G	UNK_F_TYPE	e5v1xG1	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: UNK_F_TYPE	ECOD (1.6)
G	Aminotran_5_N	e5v1xG2	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
H	UNK_F_TYPE	e5v1xH1	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: UNK_F_TYPE	ECOD (1.6)
H	Aminotran_5_N	e5v1xH2	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth E], B [auth F], C [auth D], D [auth C], E [auth A], A [auth E], B [auth F], C [auth D], D [auth C], E [auth A], F [auth B], G, H	PF00266	Aminotransferase class-V (Aminotran_5)	Aminotransferase class-V	This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth E], B [auth F], C [auth D], D [auth C], E [auth A], A [auth E], B [auth F], C [auth D], D [auth C], E [auth A], F [auth B], G, H	Hercynylcysteine sulfoxide lyase	carbon-sulfur lyase activity lyase activity hercynylcysteine sulfoxide lyase activity (ergothioneine-forming) catalytic activity	-	cellular anatomical structure intracellular anatomical structure cytoplasm membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth E], B [auth F], C [auth D], D [auth C], E [auth A], A [auth E], B [auth F], C [auth D], D [auth C], E [auth A], F [auth B], G, H	IPR015424	Pyridoxal phosphate-dependent transferase	Homologous Superfamily
A [auth E], B [auth F], C [auth D], D [auth C], E [auth A], A [auth E], B [auth F], C [auth D], D [auth C], E [auth A], F [auth B], G, H	IPR015421	Pyridoxal phosphate-dependent transferase, major domain	Homologous Superfamily
A [auth E], B [auth F], C [auth D], D [auth C], E [auth A], A [auth E], B [auth F], C [auth D], D [auth C], E [auth A], F [auth B], G, H	IPR000192	Aminotransferase class V domain	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A [auth E], B [auth F], C [auth D], D [auth C], E [auth A], A [auth E], B [auth F], C [auth D], D [auth C], E [auth A], F [auth B], G, H	LLP	Parent Component: LYS RESID: AA0119 PSI-MOD : N6-pyridoxal phosphate-L-lysine MOD:00128

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.