2AGZ

Crystal structure of the carbinolamine intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. F222 form

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
Protein Modification Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth D]	d2agzd_	Small proteins	Methylamine dehydrogenase, L chain	Methylamine dehydrogenase, L chain	automated matches	automated matches	(Alcaligenes faecalis ) [TaxId: 511 ],	SCOPe (2.08)
B [auth H]	d2agzh_	Small proteins	Methylamine dehydrogenase, L chain	Methylamine dehydrogenase, L chain	automated matches	automated matches	(Alcaligenes faecalis ) [TaxId: 511 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth D]	SCOP2B Superfamily	Methylamine dehydrogenase, L chain	8078565	3000932	SCOP2B (2022-06-29)
B [auth H]	SCOP2 Family	Methylamine dehydrogenase, L chain	8078564	4003481	SCOP2 (2022-06-29)
B [auth H]	SCOP2 Superfamily	Methylamine dehydrogenase, L chain	8078565	3000932	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)
C [auth A]	Me-amine-dh_H	e2agzA1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: Me-amine-dh_H	ECOD (1.6)
D [auth B]	Me-amine-dh_H	e2agzB1	A: beta duplicates or obligate multimers	X: beta-propeller-like	H: beta-propeller	T: 7-bladed	F: Me-amine-dh_H	ECOD (1.6)
A [auth D]	Me-amine-dh_L	e2agzD1	A: few secondary structure elements	X: Methylamine dehydrogenase, L chain (From Topology)	H: Methylamine dehydrogenase, L chain (From Topology)	T: Methylamine dehydrogenase, L chain	F: Me-amine-dh_L	ECOD (1.6)
B [auth H]	Me-amine-dh_L	e2agzH1	A: few secondary structure elements	X: Methylamine dehydrogenase, L chain (From Topology)	H: Methylamine dehydrogenase, L chain (From Topology)	T: Methylamine dehydrogenase, L chain	F: Me-amine-dh_L	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C [auth A]	2.130.10.10	Mainly Beta	7 Propeller	Methylamine Dehydrogenase	Chain H	CATH (4.3.0)
D [auth B]	2.130.10.10	Mainly Beta	7 Propeller	Methylamine Dehydrogenase	Chain H	CATH (4.3.0)
A [auth D]	2.60.30.10	Mainly Beta	Sandwich	Electron Transport Ethylamine Dehydrogenase	Methylamine/Aralkylamine dehydrogenase light chain	CATH (4.3.0)
B [auth H]	2.60.30.10	Mainly Beta	Sandwich	Electron Transport Ethylamine Dehydrogenase	Methylamine/Aralkylamine dehydrogenase light chain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
C [auth A], D [auth B]	PF06433	Methylamine dehydrogenase heavy chain (MADH) (Me-amine-dh_H)	Methylamine dehydrogenase heavy chain (MADH)	-	Repeat
A [auth D], B [auth H]	PF02975	Methylamine dehydrogenase, L chain (Me-amine-dh_L)	Methylamine dehydrogenase, L chain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
C [auth A], D [auth B]	Aromatic amine dehydrogenase	oxidoreductase activity, acting on the CH-NH2 group of donors oxidoreductase activity catalytic activity aliphatic amine dehydrogenase activity aralkylamine dehydrogenase (azurin) activity oxidoreductase activity, acting on the CH-NH2 group of donors, with a copper protein as acceptor	-	cellular anatomical structure periplasmic space
A [auth D], B [auth H]	Aromatic amine dehydrogenase	oxidoreductase activity, acting on the CH-NH2 group of donors oxidoreductase activity catalytic activity aliphatic amine dehydrogenase activity aralkylamine dehydrogenase (azurin) activity oxidoreductase activity, acting on the CH-NH2 group of donors, with a copper protein as acceptor	amine metabolic process metabolic process cellular process	cellular anatomical structure periplasmic space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
C [auth A], D [auth B]	IPR009451	Amine dehydrogenase heavy chain	Family
C [auth A], D [auth B]	IPR011044	Quinoprotein amine dehydrogenase, beta chain-like	Homologous Superfamily
C [auth A], D [auth B]	IPR015943	WD40/YVTN repeat-like-containing domain superfamily	Homologous Superfamily
A [auth D], B [auth H]	IPR006311	Twin-arginine translocation pathway, signal sequence	Conserved Site
A [auth D], B [auth H]	IPR016008	Amine dehydrogenase light chain	Family
A [auth D], B [auth H]	IPR036560	Methylamine/Aralkylamine dehydrogenase light chain superfamily	Homologous Superfamily
A [auth D], B [auth H]	IPR013504	Methylamine/Aralkylamine dehydrogenase light chain, C-terminal domain	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A [auth D], B [auth H]	TRQ	Parent Component: TRP RESID: AA0148 PSI-MOD : oxidation of tryptophan to L-tryptophyl quinone MOD:00157

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.