Research workbench
Crystal structure of the histidine racemase cntk in cobalt and nickel transporter system of staphylococcus aureus
Analyse Crystal structure of the histidine racemase cntk in cobalt and nickel… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JIS
- 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
- CS, CL
- Pockets
- 1 · best druggability 0.69
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
- CS · Cesium ion · metal · 7 copies · chains A
- CL · Chloride ion · ion · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · 4 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 | 453 | 0.69 | 0.80 | 54 | EDO, CS |
Compared structures
- 6JIS · Crystal structure of the histidine racemase CntK in cobalt and nickel transporter system… · 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 6JIS · PDBe 6JIS · UniProt A0A389TBD7
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