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 SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
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) |
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) |
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
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) |
A [auth D] | SCOP2B Superfamily | Methylamine dehydrogenase, L chain | 8078565 | 3000932 | 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 [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) |
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) |
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) |
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) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
B [auth H] | 2.60.30.10 | Mainly Beta | Sandwich | Electron Transport Ethylamine Dehydrogenase | Methylamine/Aralkylamine dehydrogenase light chain | 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) |
D [auth B] | 2.130.10.10 | Mainly Beta | 7 Propeller | Methylamine Dehydrogenase | Chain H | CATH (4.3.0) |
C [auth A] | 2.130.10.10 | Mainly Beta | 7 Propeller | Methylamine Dehydrogenase | Chain H | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
A [auth D], B [auth H] | PF02975 | Methylamine dehydrogenase, L chain (Me-amine-dh_L) | Methylamine dehydrogenase, L chain | - | Domain |
C [auth A], D [auth B] | PF06433 | Methylamine dehydrogenase heavy chain (MADH) (Me-amine-dh_H) | Methylamine dehydrogenase heavy chain (MADH) | - | Repeat |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
Chains | Polymer | Molecular Function | Biological Process | Cellular Component |
---|---|---|---|---|
A [auth D], B [auth H] | Aromatic amine dehydrogenase | |||
C [auth A], D [auth B] | Aromatic amine dehydrogenase | - |
InterPro: Protein Family Classification InterPro Database Homepage
Protein Modification Annotation
Modified Residue(s) | ||
---|---|---|
Chain | Residue(s) | Description |
A [auth D], B [auth H] | TRQ | Parent Component: TRP :  AA0148 :  oxidation of tryptophan to L-tryptophyl quinone MOD:00157 |