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Crystal structure of putative acetolactate synthase- small subunit from nitrosomonas europaea
Analyse Crystal structure of putative acetolactate synthase- small subunit from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2PC6
- Type
- protein
- Length
- 653 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Probable acetolactate synthase isozyme III (small subunit)
- EC
- 4.1.3.18
- UniProt
- Q82UZ2
- Ligands
- UNL, CA
- Pockets
- 7 · best druggability 0.73
Structure
x-ray diffraction · 3 distinct chains · 32% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | Probable acetolactate synthase isozyme III (small subunit) (EC 4.1.3.18) | protein | 164 | 32% helix, 41% strand | Q82UZ2 |
| B | Probable acetolactate synthase isozyme III (small subunit) (EC 4.1.3.18) | protein | 163 | 34% helix, 40% strand | Q82UZ2 |
| D | Probable acetolactate synthase isozyme III (small subunit) (EC 4.1.3.18) | protein | 162 | 30% helix, 40% strand | Q82UZ2 |
Ligands and binding sites
- UNL · Unknown ligand · ligand · 3 copies · chains A, B, D
- CA · Calcium ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 755 | 0.73 | 0.78 | 85 | empty |
| 2 | 50 | 0.40 | 0.82 | 18 | empty |
| 3 | 117 | 0.38 | 0.74 | 21 | empty |
| 4 | 85 | 0.37 | 0.76 | 23 | empty |
| 5 | 90 | 0.33 | 0.74 | 20 | empty |
Interfaces
5 interfaces between chains.
- A–C · 2350 Ų buried · 40 hydrogen bonds · protein-protein
- B–D · 2328 Ų buried · 34 hydrogen bonds · protein-protein
- B–C · 404 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 174 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 18 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 modified (engineered).
Compared structures
- 2PC6 · Crystal structure of putative acetolactate synthase- small subunit from Nitrosomonas… · 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 Q82UZ2
- Elsewhere: RCSB PDB 2PC6 · PDBe 2PC6 · UniProt Q82UZ2
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