MolNFT v1 · #17632 · protein
The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an unusual intermediate.
1OZH · Acetolactate synthase, catabolic: “The crystal structure of klebsiella pneumoniae acetolactate synthase with enzyme-bound cofactor and with an…”. X-ray diffraction, 3 ligands (HE3, MG, PO4), 15 pockets (best druggability 0.84).…
- PDB
- 1OZH
- Type
- protein
- Length
- 2,171 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetolactate synthase, catabolic
- EC
- 4.1.3.18
- UniProt
- P27696
- Ligands
- HE3, MG, PO4
- Pockets
- 15 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 44% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetolactate synthase, catabolic (EC 4.1.3.18) | protein | 545 | 44% helix, 20% strand | P27696 |
| B | Acetolactate synthase, catabolic (EC 4.1.3.18) | protein | 545 | 43% helix, 19% strand | P27696 |
| C | Acetolactate synthase, catabolic (EC 4.1.3.18) | protein | 543 | 44% helix, 19% strand | P27696 |
| D | Acetolactate synthase, catabolic (EC 4.1.3.18) | protein | 538 | 45% helix, 19% strand | P27696 |
Ligands and binding sites
- HE3 · 2-hydroxyethyl dihydrothiachrome diphosphate · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
- PO4 · Phosphate ion · ion · 4 copies · chains A, B, C, D
- PEG · Di(hydroxyethyl)ether · additive · 5 copies · chains A, B, C, D
- PGE · Triethylene glycol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1019 | 0.84 | 0.84 | 107 | MG, HE3 |
| 2 | 868 | 0.82 | 0.84 | 95 | MG, HE3 |
| 3 | 885 | 0.82 | 0.84 | 90 | HE3 |
| 4 | 959 | 0.81 | 0.82 | 130 | empty |
| 5 | 211 | 0.77 | 0.92 | 37 | MG, HE3 |
Interfaces
6 interfaces between chains.
- C–D · 2753 Ų buried · 42 hydrogen bonds · protein-protein
- A–B · 2693 Ų buried · 41 hydrogen bonds · protein-protein
- A–D · 1256 Ų buried · 29 hydrogen bonds · protein-protein
- B–C · 1016 Ų buried · 22 hydrogen bonds · protein-protein
- A–C · 187 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1OZH · The crystal structure of Klebsiella pneumoniae acetolactate synthase with enzyme-bound… · the same entry in another collection · chain D against D, TM-score 1.00
- P27696 · AlphaFold monomer V2.0 prediction for acetolactate synthase, catabolic (P27696) · a predicted model of the same protein · chain D against A, TM-score 0.96
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 P27696
- Elsewhere: RCSB PDB 1OZH · PDBe 1OZH · UniProt P27696
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