6CXH

Crystal structure of particulate methane monooxygenase from Methylomicrobium alcaliphilum 20Z

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Membrane Protein Annotation: OPM
Membrane Protein Annotation: PDBTM
Membrane Protein Annotation: MemProtMD

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Monooxygenase subunit B transmembrane domain-like	8095946	4007811	SCOP2 (2022-06-29)
A	SCOP2 Family	Monooxygenase subunit B C-terminal domain-like	8095947	4007812	SCOP2 (2022-06-29)
A	SCOP2 Family	Monooxygenase subunit B copper-binding domain-like	8061309	4005056	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Monooxygenase subunit B transmembrane domain-like	8095949	3002711	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Monooxygenase subunit B C-terminal domain-like	8095950	3002712	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PapD-like	8095948	3002067	SCOP2 (2022-06-29)
B	SCOP2 Family	Ammonia monooxygenase-like	8061759	4006879	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Gx transporter-like	8095954	3002268	SCOP2 (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	PF04744	e6cxhA3	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: PF04744	ECOD (1.6)
A	PF04744	e6cxhA2	A: alpha bundles	X: Long alpha-hairpin	H: PmoB helical hairpin (From Topology)	T: PmoB helical hairpin	F: PF04744	ECOD (1.6)
B	PF02461	e6cxhB1	A: alpha bundles	X: PmoA (From Topology)	H: PmoA (From Topology)	T: PmoA	F: PF02461	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.120.570	Mainly Beta	Sandwich	Jelly Rolls	Particulate methane monooxygenase, b subunit. Chain: A, domain 1	CATH (4.3.0)
A	1.10.287.710	Mainly Alpha	Orthogonal Bundle	Helix Hairpins	Helix hairpin bin	CATH (4.3.0)
A	2.60.40.1580	Mainly Beta	Sandwich	Immunoglobulin-like	Particulate methane monooxygenase, b subunit. Chain: A, domain 3	CATH (4.3.0)
B	1.20.1450.10	Mainly Alpha	Up-down Bundle	particulate methane monooxygenase, chain B	Ammonia/particulate methane monooxygenase, subunit A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF04744	Monooxygenase subunit B protein (Monooxygenase_B)	Monooxygenase subunit B protein	-	Family
B	PF02461	Ammonia monooxygenase (AMO)	Ammonia monooxygenase	-	Family
C	PF04896	Ammonia monooxygenase/methane monooxygenase, subunit C (AmoC)	Ammonia monooxygenase/methane monooxygenase, subunit C	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Particulate methane monooxygenase, B subunit	oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen methane monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen catalytic activity methane monooxygenase NADH activity methane monooxygenase NADPH activity	-	-
B	Particulate methane monooxygenase, A subunit	oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen methane monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen catalytic activity methane monooxygenase NADH activity methane monooxygenase NADPH activity	-	membrane cellular anatomical entity
C	Particulate methane monooxygenase, C subunit	oxidoreductase activity monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen methane monooxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen catalytic activity methane monooxygenase NADH activity methane monooxygenase NADPH activity	-	membrane cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR006833	Ammonia monooxygenase/particulate methane monooxygenase, subunit B	Family
A	IPR023141	Ammonia/methane monooxygenase, subunit B, hairpin domain superfamily	Homologous Superfamily
A	IPR023303	Ammonia/methane monooxygenase, subunit B, C-terminal	Homologous Superfamily
A	IPR023301	Ammonia/methane monooxygenase, subunitB, N-terminal	Homologous Superfamily
B	IPR037001	Ammonia/particulate methane monooxygenase, subunit A superfamily	Homologous Superfamily
B	IPR003393	Ammonia monooxygenase/particulate methane monooxygenase, subunit A	Family
C	IPR006980	Ammonia monooxygenase/particulate methane monooxygenase, subunit C	Family
C	IPR023349	Ammonia monooxygenase/particulate methane monooxygenase, subunit C domain superfamily	Homologous Superfamily

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B, C	OPM				Methane monooxygenase

Membrane Protein Annotation: PDBTM PDBTM Database Homepage

Chains	External Link	Comment
A, B, C	PDBTM	Annotated as membrane protein by PDBTM

Membrane Protein Annotation: MemProtMD MemProtMD Database Homepage

Chains	External Link	Comment
A, B, C	MemProtMD	Annotated as membrane protein by MemProtMD

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.