Research workbench
277 K cryoem structure of sso-kari in complex with magnesium ions
Analyse 277 K cryoem structure of sso-kari in complex with magnesium ions in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KOU
- Type
- protein
- Length
- 3,936 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ketol-acid reductoisomerase
- UniProt
- A0A157T175
- Ligands
- MG
- Pockets
- 20 · best druggability 0.78
Structure
electron microscopy · 1 distinct chain · 55% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Ketol-acid reductoisomerase | protein | 328 | 55% helix, 12% strand | A0A157T175 |
Ligands and binding sites
- MG · Magnesium ion · metal · 24 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 759 | 0.78 | 0.82 | 70 | MG |
| 2 | 942 | 0.78 | 0.80 | 75 | MG |
| 3 | 871 | 0.78 | 0.81 | 71 | MG |
| 4 | 708 | 0.78 | 0.82 | 49 | MG |
| 5 | 953 | 0.77 | 0.80 | 82 | MG |
Interfaces
30 interfaces between chains.
- C–D · 5670 Ų buried · 33 hydrogen bonds · protein-protein
- I–J · 5663 Ų buried · 32 hydrogen bonds · protein-protein
- E–F · 5663 Ų buried · 33 hydrogen bonds · protein-protein
- A–B · 5660 Ų buried · 34 hydrogen bonds · protein-protein
- K–L · 5657 Ų buried · 33 hydrogen bonds · protein-protein
Compared structures
- 6KOU · 277 K cryoEM structure of Sso-KARI in complex with magnesium ions · 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 A0A157T175
- Elsewhere: RCSB PDB 6KOU · PDBe 6KOU · UniProt A0A157T175
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