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The crystal structure of the staphylococcus aureus fatty acid kinase (fak) B1 protein loaded with 14-methylhexadecanoic acid (anteiso C17:0) to 1.93 ångström resolution
Analyse The crystal structure of the staphylococcus aureus fatty acid kinase (fak) B1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B9I
- Type
- protein
- Length
- 561 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- X5EH37
- Ligands
- D0G, NA
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 283 | — | X5EH37 |
| B | — | protein | 278 | — | X5EH37 |
Ligands and binding sites
- D0G · (14S)-14-methylhexadecanoic acid · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · 2 copies · chains B
- GOL · Glycerol · additive · 11 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6B9I · The crystal structure of the Staphylococcus aureus Fatty acid Kinase (Fak) B1 protein… · 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 X5EH37
- Elsewhere: RCSB PDB 6B9I · PDBe 6B9I · UniProt X5EH37
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