Research workbench
The crystal structure of the staphylococcus aureus fatty acid kinase (fak) B1 protein A121I mutant to 2.02 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
- 6MH9
- Type
- protein
- Length
- 569 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
- PLM
- Pockets
- 9 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acid kinase (fak) B1 protein | protein | 288 | 42% helix, 25% strand | X5EH37 |
| B | Fatty acid kinase (fak) B1 protein | protein | 281 | 41% helix, 24% strand | X5EH37 |
Ligands and binding sites
- PLM · Palmitic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 120 | 0.77 | 0.96 | 28 | PLM |
| 2 | 460 | 0.69 | 0.80 | 55 | PLM |
| 3 | 217 | 0.58 | 0.79 | 34 | empty |
| 4 | 371 | 0.56 | 0.75 | 39 | empty |
| 5 | 160 | 0.48 | 0.77 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 316 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6MH9 · 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 6MH9 · PDBe 6MH9 · UniProt X5EH37
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