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N-acyl amino acid racemase from amycolatopsis sp. ts-1-60: G291D F323 mutant in complex with N-acetyl phenylalanine
Analyse N-acyl amino acid racemase from amycolatopsis sp. ts-1-60: G291D F323 mutant in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FJT
- Type
- protein
- Length
- 1,473 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q44244
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 368 | — | Q44244 |
| D | — | protein | 369 | — | Q44244 |
Compared structures
- 5FJT · N-acyl amino acid racemase from Amycolatopsis sp. Ts-1-60: G291D F323 mutant in complex… · the same entry in another collection · chain D against D, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q44244
- Elsewhere: RCSB PDB 5FJT · PDBe 5FJT · UniProt Q44244
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