7A0C

X-ray structure of NikA from Escherichia coli in complex with Fe-6-Me2-BPMCN

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
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	d7a0cb_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Nickel-binding periplasmic protein NikA	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
A	d7a0ca_	Alpha and beta proteins (a/b)	Periplasmic binding protein-like II	Periplasmic binding protein-like II	Phosphate binding protein-like	Nickel-binding periplasmic protein NikA	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Type 2 solute binding protein-like	8035860	3000083	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Type 2 solute binding protein-like	8035860	3000083	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)
B	SBP_bac_5_1st	e7a0cB1	A: a+b two layers	X: Alpha-beta plaits	H: Oligo-peptide binding protein (OPPA) insertion domain (From Topology)	T: Oligo-peptide binding protein (OPPA) insertion domain	F: SBP_bac_5_1st	ECOD (1.6)
B	SBP_bac_5_3rd	e7a0cB2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_5_3rd	ECOD (1.6)
B	SBP_bac_5_2nd	e7a0cB3	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_5_2nd	ECOD (1.6)
A	SBP_bac_5_1st	e7a0cA3	A: a+b two layers	X: Alpha-beta plaits	H: Oligo-peptide binding protein (OPPA) insertion domain (From Topology)	T: Oligo-peptide binding protein (OPPA) insertion domain	F: SBP_bac_5_1st	ECOD (1.6)
A	SBP_bac_5_3rd	e7a0cA2	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_5_3rd	ECOD (1.6)
A	SBP_bac_5_2nd	e7a0cA1	A: a/b three-layered sandwiches	X: Periplasmic binding protein-like II (From Topology)	H: Periplasmic binding protein-like II (From Topology)	T: Periplasmic binding protein-like II	F: SBP_bac_5_2nd	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00496	Bacterial extracellular solute-binding proteins, family 5 Middle (SBP_bac_5)	Bacterial extracellular solute-binding proteins, family 5 Middle	The borders of this family are based on the PDBSum definitions of the domain edges for Swiss:P06202.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Nickel-binding periplasmic protein	cation binding transition metal ion binding ion binding binding nickel cation binding metal ion binding small molecule binding peptide transmembrane transporter activity transporter activity transmembrane transporter activity organic cyclic compound binding tetrapyrrole binding heme binding metal cluster binding	chemotaxis negative chemotaxis response to stimulus taxis response to chemical response to external stimulus locomotion peptide transport localization nitrogen compound transport amide transport transport establishment of localization nickel cation transport chemotaxis negative chemotaxis response to stimulus taxis response to chemical response to external stimulus locomotion peptide transport localization nitrogen compound transport amide transport transport establishment of localization nickel cation transport transition metal ion transport monoatomic ion transport monoatomic cation transport metal ion transport import into cell nickel cation transmembrane transport import across plasma membrane monoatomic ion transmembrane transport inorganic ion transmembrane transport inorganic cation import across plasma membrane inorganic cation transmembrane transport transmembrane transport monoatomic cation transmembrane transport inorganic ion import across plasma membrane nickel cation import across plasma membrane cellular process	cellular anatomical structure membrane ATPase dependent transmembrane transport complex ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing protein-containing complex plasma membrane protein complex plasma membrane membrane protein complex transporter complex ATP-binding cassette (ABC) transporter complex cell periphery transmembrane transporter complex periplasmic space outer membrane-bounded periplasmic space cellular anatomical structure membrane ATPase dependent transmembrane transport complex ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing protein-containing complex plasma membrane protein complex plasma membrane membrane protein complex transporter complex ATP-binding cassette (ABC) transporter complex cell periphery transmembrane transporter complex periplasmic space outer membrane-bounded periplasmic space cell envelope

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR011980	Metal-staphylopine-binding protein CntA-like	Family
A, B	IPR030678	Peptide/nickel binding protein, MppA-type	Family
A, B	IPR023765	Solute-binding protein family 5, conserved site	Conserved Site
A, B	IPR000914	Solute-binding protein family 5 domain	Domain
A, B	IPR039424	Solute-binding protein family 5	Family

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.