Research workbench
The crystal structure of the staphylococcus aureus fatty acid kinase (fak) B1 protein A158L mutant to 2.33 ångström resolution exhibits a conformation change compared to the wild type form
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
- 6NM1
- Type
- protein
- Length
- 573 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid kinase (fak) B1 protein
- UniProt
- X5EH37
- Ligands
- MYR
- Pockets
- 10 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acid kinase (fak) B1 protein | protein | 288 | 43% helix, 24% strand | X5EH37 |
| B | Fatty acid kinase (fak) B1 protein | protein | 285 | 36% helix, 24% strand | X5EH37 |
Ligands and binding sites
- MYR · Myristic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.78 | 0.95 | 28 | MYR |
| 2 | 290 | 0.62 | 0.79 | 41 | MYR |
| 3 | 334 | 0.59 | 0.77 | 36 | empty |
| 4 | 248 | 0.52 | 0.76 | 35 | empty |
| 5 | 188 | 0.50 | 0.77 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 324 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6NM1 · 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 6NM1 · PDBe 6NM1 · UniProt X5EH37
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