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Brassica napus enoyl acp reductase A138G mutant complexed with NAD+ and thienodiazaborine
Analyse Brassica napus enoyl acp reductase A138G mutant complexed with NAD+ and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CWU
- Type
- protein
- Length
- 592 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P80030
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 296 | — | P80030 |
Compared structures
- 1CWU · Brassica napus enoyl acp reductase A138G mutant complexed with NAD+ and thienodiazaborine · the same entry in another collection · chain A against A, TM-score 1.00
- P80030 · AlphaFold monomer V2.0 prediction for enoyl-[acyl-carrier-protein] reductase [NADH]… · a predicted model of the same protein · chain B against A, 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 P80030
- Elsewhere: RCSB PDB 1CWU · PDBe 1CWU · UniProt P80030
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