Research workbench
Crystal structure of S. aureus cntk with C72S mutation
Analyse Crystal structure of S. aureus cntk with C72S mutation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JIW
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Diaminopimelate epimerase
- UniProt
- A0A389TBD7
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 24% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Diaminopimelate epimerase | protein | 263 | 24% helix, 44% strand | A0A389TBD7 |
Ligands and binding sites
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 | 397 | 0.65 | 0.79 | 43 | SO4 |
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 6JIW · Crystal structure of S. aureus CntK with C72S mutation · 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 6JIW · PDBe 6JIW · UniProt A0A389TBD7
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