Research workbench
The X-ray crystal structure of the N-terminal domain of staphylococcus aureus fatty acid kinase a (faka, residues 1-208) in complex with AMP and ADP to 1.105 ångström resolution
Analyse The X-ray crystal structure of the N-terminal domain of staphylococcus aureus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7SNB
- Type
- protein
- Length
- 222 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fatty acid kinase a
- UniProt
- Q7A5Z4
- Ligands
- AMP, ADP, MG
- Pockets
- 1 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 68% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fatty acid kinase a | protein | 222 | 68% helix, 1% strand | Q7A5Z4 |
Ligands and binding sites
- AMP · Adenosine monophosphate · ligand · chains A
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · 4 copies · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 146 | 0.59 | 0.83 | 23 | AMP, ADP, MG |
Compared structures
- 7SNB · The X-ray crystal structure of the N-terminal domain of Staphylococcus aureus Fatty Acid… · the same entry in another collection · chain A against A, TM-score 1.00
- Q7A5Z4 · AlphaFold monomer V2.0 prediction for uncharacterized protein SA1069 (Q7A5Z4) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 Q7A5Z4
- Elsewhere: RCSB PDB 7SNB · PDBe 7SNB · UniProt Q7A5Z4
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