Research workbench
Crystal structure of a high molecular weight 3-oxoacyl-acp reductase (fabg) from acinetobacter baumannii crystal form 1
Analyse Crystal structure of a high molecular weight 3-oxoacyl-acp reductase (fabg)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UUV
- Type
- protein
- Length
- 879 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A219C8F5
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 438 | — | A0A219C8F5 |
| B | — | protein | 441 | — | A0A219C8F5 |
Compared structures
- 6UUV · Crystal structure of a high molecular weight 3-oxoacyl-ACP reductase (FabG) from… · 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 A0A219C8F5
- Elsewhere: RCSB PDB 6UUV · PDBe 6UUV · UniProt A0A219C8F5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.