5X1Y

Structure of mercuric reductase from Lysinibacillus sphaericus

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A [auth B]	PF02852	e5x1yB2	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain (From Topology)	T: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain	F: PF02852	ECOD (1.6)
A [auth B]	PF07992	e5x1yB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF07992	ECOD (1.6)
B [auth A]	PF02852	e5x1yA1	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain (From Topology)	T: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain	F: PF02852	ECOD (1.6)
B [auth A]	PF07992	e5x1yA3	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF07992	ECOD (1.6)
C	PF02852	e5x1yC3	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain (From Topology)	T: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain	F: PF02852	ECOD (1.6)
C	PF07992	e5x1yC2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF07992	ECOD (1.6)
D	PF02852	e5x1yD2	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain (From Topology)	T: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain	F: PF02852	ECOD (1.6)
D	PF07992	e5x1yD1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF07992	ECOD (1.6)
E	PF02852	e5x1yE1	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain (From Topology)	T: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain	F: PF02852	ECOD (1.6)
E	PF07992	e5x1yE2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF07992	ECOD (1.6)
F	PF02852	e5x1yF3	A: a+b two layers	X: FAD-linked reductases, C-terminal domain-like	H: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain (From Topology)	T: FAD/NAD-linked reduatases, dimerisation (C-terminal) domain	F: PF02852	ECOD (1.6)
F	PF07992	e5x1yF1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: FAD/NAD(P)-binding domain	F: PF07992	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth B]	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
A [auth B]	3.30.390.30	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
B [auth A]	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
B [auth A]	3.30.390.30	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
C	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
C	3.30.390.30	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
D	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
D	3.30.390.30	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
E	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
E	3.30.390.30	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
F	3.50.50.60	Alpha Beta	3-Layer(bba) Sandwich	FAD/NAD(P)-binding domain	FAD/NAD(P)-binding domain	CATH (4.3.0)
F	3.30.390.30	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth A], C, D, E, A [auth B], B [auth A], C, D, E, F	PF07992	Pyridine nucleotide-disulphide oxidoreductase (Pyr_redox_2)	Pyridine nucleotide-disulphide oxidoreductase	This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.	Domain
A [auth B], B [auth A], C, D, E, A [auth B], B [auth A], C, D, E, F	PF02852	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain (Pyr_redox_dim)	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain	This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth A], C, D, E, A [auth B], B [auth A], C, D, E, F	Mercuric reductase	binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding oxidoreductase activity, acting on metal ions oxidoreductase activity oxidoreductase activity, acting on metal ions, NAD or NADP as acceptor catalytic activity mercury (II) reductase activity binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding oxidoreductase activity, acting on metal ions oxidoreductase activity oxidoreductase activity, acting on metal ions, NAD or NADP as acceptor catalytic activity mercury (II) reductase activity flavin adenine dinucleotide binding ion binding anion binding cation binding transition metal ion binding mercury ion binding metal ion binding oxidoreductase activity, acting on a sulfur group of donors oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor	detoxification of inorganic compound response to mercury ion response to stimulus response to metal ion response to chemical detoxification detoxification of mercury ion response to inorganic substance response to toxic substance	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth A], C, D, E, A [auth B], B [auth A], C, D, E, F	IPR004099	Pyridine nucleotide-disulphide oxidoreductase, dimerisation domain	Domain
A [auth B], B [auth A], C, D, E, A [auth B], B [auth A], C, D, E, F	IPR006121	Heavy metal-associated domain, HMA	Domain
A [auth B], B [auth A], C, D, E, A [auth B], B [auth A], C, D, E, F	IPR001100	Pyridine nucleotide-disulphide oxidoreductase, class I	Family
A [auth B], B [auth A], C, D, E, A [auth B], B [auth A], C, D, E, F	IPR016156	FAD/NAD-linked reductase, dimerisation domain superfamily	Homologous Superfamily
A [auth B], B [auth A], C, D, E, A [auth B], B [auth A], C, D, E, F	IPR036188	FAD/NAD(P)-binding domain superfamily	Homologous Superfamily
A [auth B], B [auth A], C, D, E, A [auth B], B [auth A], C, D, E, F	IPR021179	Mercury(II) reductase	Family
A [auth B], B [auth A], C, D, E, A [auth B], B [auth A], C, D, E, F	IPR023753	FAD/NAD(P)-binding domain	Domain
A [auth B], B [auth A], C, D, E, A [auth B], B [auth A], C, D, E, F	IPR036163	Heavy metal-associated domain superfamily	Homologous Superfamily
A [auth B], B [auth A], C, D, E, A [auth B], B [auth A], C, D, E, F	IPR012999	Pyridine nucleotide-disulphide oxidoreductase, class I, active site	Active Site

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 R01GM133198.