Research workbench
298 K cryoem structure of sso-kari in complex with MG2+, NADH and cpd
Analyse 298 K cryoem structure of sso-kari in complex with MG2+, NADH and cpd in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KPJ
- 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
- NAI, 9TY, MG
- Pockets
- 20 · best druggability 0.79
Structure
electron microscopy · 1 distinct chain · 56% helix, 11% 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 | 56% helix, 11% strand | A0A157T175 |
Ligands and binding sites
- NAI · 1,4-dihydronicotinamide adenine dinucleotide · ligand · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
- 9TY · cyclopropane-1,1-dicarboxylic acid · ligand · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
- 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 | 908 | 0.79 | 0.81 | 90 | NAI, 9TY |
| 2 | 770 | 0.79 | 0.82 | 85 | MG, NAI, 9TY |
| 3 | 789 | 0.78 | 0.82 | 81 | NAI, 9TY |
| 4 | 840 | 0.78 | 0.81 | 86 | MG, NAI, 9TY |
| 5 | 917 | 0.78 | 0.80 | 85 | MG, NAI, 9TY |
Interfaces
30 interfaces between chains.
- K–L · 5577 Ų buried · 28 hydrogen bonds · protein-protein
- G–H · 5563 Ų buried · 28 hydrogen bonds · protein-protein
- E–F · 5557 Ų buried · 28 hydrogen bonds · protein-protein
- I–J · 5545 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 5540 Ų buried · 24 hydrogen bonds · protein-protein
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 6KPJ · PDBe 6KPJ · UniProt A0A157T175
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.