Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad
External Resource: Annotation
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
A | SCOP2 Family | Arylamine N-acetyltransferase | 8067821 | 4000879 | SCOP2 (2022-06-29) |
A | SCOP2 Superfamily | Cysteine proteinases | 8067822 | 3001808 | SCOP2 (2022-06-29) |
B | SCOP2B Superfamily | Cysteine proteinases | 8067822 | 3001808 | SCOP2B (2022-06-29) |
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
A | Acetyltransf_2 | e4dmoA1 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: Acetyltransf_2 | ECOD (1.6) |
B | Acetyltransf_2 | e4dmoB1 | A: a+b complex topology | X: Cysteine proteinases-like | H: Cysteine proteinases (From Topology) | T: Cysteine proteinases | F: Acetyltransf_2 | ECOD (1.6) |
Chains | Polymer | Molecular Function | Biological Process | Cellular Component |
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| N-hydroxyarylamine O-acetyltransferase | | - | - |