Annotations: 8DBX

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Helical backbone metal receptor	8043190	3001679	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Helical backbone metal receptor	8043190	3001679	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Helical backbone metal receptor	8043192	3001679	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Helical backbone metal receptor	8043192	3001679	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	Oxidored_nitro_3rd	e8dbxA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Chelatase-like	F: Oxidored_nitro_3rd	ECOD (1.6)
C	Oxidored_nitro_3rd	e8dbxC3	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Chelatase-like	F: Oxidored_nitro_3rd	ECOD (1.6)
B	F_UNCLASSIFIED	e8dbxB3	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Chelatase-like	F: F_UNCLASSIFIED	ECOD (1.6)
B	Oxidored_nitro_3rd	e8dbxB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Chelatase-like	F: Oxidored_nitro_3rd	ECOD (1.6)
B	Oxidored_nitro_1st	e8dbxB2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Chelatase-like	F: Oxidored_nitro_1st	ECOD (1.6)
D	F_UNCLASSIFIED	e8dbxD1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Chelatase-like	F: F_UNCLASSIFIED	ECOD (1.6)
D	Oxidored_nitro_3rd	e8dbxD2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Chelatase-like	F: Oxidored_nitro_3rd	ECOD (1.6)
D	Oxidored_nitro_1st	e8dbxD3	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Class I glutamine amidotransferase-like	T: Chelatase-like	F: Oxidored_nitro_1st	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C	PF00148	Nitrogenase component 1 type Oxidoreductase (Oxidored_nitro)	Nitrogenase component 1 type Oxidoreductase		Domain
B, D	PF00148	Nitrogenase component 1 type Oxidoreductase (Oxidored_nitro)	Nitrogenase component 1 type Oxidoreductase		Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C	Nitrogenase molybdenum-iron protein alpha chain	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding iron-sulfur cluster binding metal cluster binding cation binding metal ion binding oxidoreductase activity nitrogenase activity oxidoreductase activity, acting on iron-sulfur proteins as donors catalytic activity oxidoreductase activity, acting on iron-sulfur proteins as donors, dinitrogen as acceptor	nitrogen cycle metabolic process metabolic process cellular process nitrogen fixation	protein-containing complex molybdenum-iron nitrogenase complex catalytic complex nitrogenase complex oxidoreductase complex intracellular protein-containing complex
B, D	Nitrogenase molybdenum-iron protein beta chain	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding iron-sulfur cluster binding metal cluster binding cation binding metal ion binding oxidoreductase activity nitrogenase activity oxidoreductase activity, acting on iron-sulfur proteins as donors catalytic activity oxidoreductase activity, acting on iron-sulfur proteins as donors, dinitrogen as acceptor	nitrogen cycle metabolic process metabolic process cellular process nitrogen fixation	protein-containing complex molybdenum-iron nitrogenase complex catalytic complex nitrogenase complex oxidoreductase complex intracellular protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C	IPR000510	Nitrogenase/oxidoreductase, component 1	Domain
A, C	IPR005972	Nitrogenase molybdenum-iron protein alpha chain	Family
A, C	IPR000318	Nitrogenase component 1, conserved site	Conserved Site
A, C	IPR010143	Nitrogenase component 1, alpha chain	Family
B, D	IPR000510	Nitrogenase/oxidoreductase, component 1	Domain
B, D	IPR005976	Nitrogenase molybdenum-iron protein beta chain	Family
B, D	IPR000318	Nitrogenase component 1, conserved site	Conserved Site
B, D	IPR050152	ChlB/BchB/BchZ	Family
B, D	IPR024564	Nitrogenase molybdenum-iron protein beta chain, N-terminal	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 R01GM157729.