Crystal structure of L-phenylalanine oxidase from Psuedomonas sp.P501
External Resource: Annotation
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
B | EUF08303 | e2yr6B2 | A: a+b two layers | X: FAD-linked reductases, C-terminal domain-like | H: FAD-linked reductases-C (From Topology) | T: FAD-linked reductases-C | F: EUF08303 | ECOD (1.6) |
B | Amino_oxidase_1st | e2yr6B1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: FAD/NAD(P)-binding domain | F: Amino_oxidase_1st | ECOD (1.6) |
A | EUF08303 | e2yr6A2 | A: a+b two layers | X: FAD-linked reductases, C-terminal domain-like | H: FAD-linked reductases-C (From Topology) | T: FAD-linked reductases-C | F: EUF08303 | ECOD (1.6) |
A | Amino_oxidase_1st | e2yr6A1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: FAD/NAD(P)-binding domain | F: Amino_oxidase_1st | ECOD (1.6) |
Chains | Polymer | Molecular Function | Biological Process | Cellular Component |
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| Pro-enzyme of L-phenylalanine oxidase | | - | - |