Research workbench
Crystal structure of S. aureus CntK in inactive state
Analyse Crystal structure of S. aureus CntK in inactive state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6L4L
- Type
- protein
- Length
- 259 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Staphylococcus aureus
- Molecule
- Diaminopimelate epimerase
- UniProt
- A0A389TBD7
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 25% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Diaminopimelate epimerase | protein | 259 | 25% helix, 44% strand | A0A389TBD7 |
Ligands and binding sites
- EDO · 1,2-ethanediol · 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 | 332 | 0.65 | 0.80 | 43 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6L4L · Crystal structure of S. aureus cntk in inactive state · 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 A0A389TBD7
- Elsewhere: RCSB PDB 6L4L · PDBe 6L4L · UniProt A0A389TBD7
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