Research workbench
Enoyl-acp reductase fabi from burkholderia pseudomallei with cofactor NADH and inhibitor PT155
Analyse Enoyl-acp reductase fabi from burkholderia pseudomallei with cofactor NADH and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4BKU
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- I1WHT9
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 257 | — | I1WHT9 |
Compared structures
- 4BKU · Enoyl-ACP reductase FabI from Burkholderia pseudomallei with cofactor NADH and inhibitor… · the same entry in another collection · chain A 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 I1WHT9
- Elsewhere: RCSB PDB 4BKU · PDBe 4BKU · UniProt I1WHT9
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