3LNN

Crystal structure of ZneB from Cupriavidus metallidurans

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d3lnnb_	Membrane and cell surface proteins and peptides	HlyD-like secretion proteins	HlyD-like secretion proteins	automated matches	automated matches	(Cupriavidus metallidurans CH34 ) [TaxId: 266264 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	HlyD-like secretion proteins	8092219	4003003	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	HlyD C-terminal domain-like	8092222	3002572	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Single hybrid motif	8092221	3001880	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	HlyD beta-barrel domain-like	8092220	3002000	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Single hybrid motif	8092221	3001880	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Single hybrid motif	8092221	3001880	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	HlyD beta-barrel domain-like	8092220	3002000	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	HlyD beta-barrel domain-like	8092220	3002000	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	F_UNCLASSIFIED	e3lnnA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF16576	e3lnnA2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: PF16576	ECOD (1.6)
A	F_UNCLASSIFIED	e3lnnA4	A: alpha bundles	X: helical hairpin of HlyD-like secretion proteins (From Topology)	H: helical hairpin of HlyD-like secretion proteins (From Topology)	T: helical hairpin of HlyD-like secretion proteins	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF13533	e3lnnA3	A: a+b complex topology	X: alpha/beta-Hammerhead/Barrel-sandwich hybrid	H: alpha/beta-Hammerhead/Barrel-sandwich hybrid	T: Single hybrid motif	F: PF13533	ECOD (1.6)
B	PF16576	e3lnnB2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: Alanine racemase-C	F: PF16576	ECOD (1.6)
B	F_UNCLASSIFIED	e3lnnB5	A: alpha bundles	X: helical hairpin of HlyD-like secretion proteins (From Topology)	H: helical hairpin of HlyD-like secretion proteins (From Topology)	T: helical hairpin of HlyD-like secretion proteins	F: F_UNCLASSIFIED	ECOD (1.6)
B	PF13533	e3lnnB3	A: a+b complex topology	X: alpha/beta-Hammerhead/Barrel-sandwich hybrid	H: alpha/beta-Hammerhead/Barrel-sandwich hybrid	T: Single hybrid motif	F: PF13533	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.420.20	Mainly Beta	Beta Barrel	conserved putative lor/sdh protein from methanococcus maripaludis s2 fold		CATH (4.3.0)
A	2.40.30.170	Mainly Beta	Beta Barrel	Elongation Factor Tu (Ef-tu)	domain 3	CATH (4.3.0)
A	2.40.50.100	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)	RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain	CATH (4.3.0)
A	1.10.287.470	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
B	2.40.30.170	Mainly Beta	Beta Barrel	Elongation Factor Tu (Ef-tu)	domain 3	CATH (4.3.0)
B	2.40.50.100	Mainly Beta	Beta Barrel	OB fold (Dihydrolipoamide Acetyltransferase, E2P)	RNA polymerase II/Efflux pump adaptor protein, barrel-sandwich hybrid domain	CATH (4.3.0)
B	1.10.287.470	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00529	Cation efflux system protein CusB domain 1 (CusB_dom_1)	Cation efflux system protein CusB domain 1	-	Family
A, B	PF16576	Barrel-sandwich domain of CusB or HlyD membrane-fusion (HlyD_D23)	Barrel-sandwich domain of CusB or HlyD membrane-fusion	HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole ...	HlyD_D23 is the combined domains 2 and 3 of the membrane-fusion proteins CusB and HlyD, which forms a barrel-sandwich. CusB and HlyD proteins are membrane fusion proteins of the CusCFBA copper efflux system in E.coli and related bacteria. The whole molecule hinges between D2 and D3. Efflux systems of this resistance-nodulation-division group - RND - have been developed to excrete poisonous metal ions, and in E.coli the only one that deals with silver and copper is the CusA transporter. The transporter CusA works in conjunction with a periplasmic component that is a membrane fusion protein, eg CusB, and an outer-membrane channel component CusC in a CusABC complex driven by import of protons.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Membrane fusion protein (MFP) heavy metal cation efflux ZneB (CzcB-like)	cation binding ion binding binding metal ion binding small molecule binding transporter activity transmembrane transporter activity	response to stimulus response to chemical	membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR006143	RND efflux pump, membrane fusion protein	Family
A, B	IPR043602	Cation efflux system protein CusB, domain 1	Domain
A, B	IPR032317	RND efflux pump, membrane fusion protein, barrel-sandwich domain	Domain

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.