Research workbench
Crystal structure of ahas holo-enzyme
Analyse Crystal structure of ahas holo-enzyme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6LPI
- Type
- protein
- Length
- 2,486 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetolactate synthase isozyme 1 small subunit; Acetolactate synthase isozyme 1 large…
- EC
- 2.2.1.6
- UniProt
- P0ADF8, P08142
- Ligands
- FAD, TPP, MG
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 7 distinct chains · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E | Acetolactate synthase isozyme 1 small subunit (EC 2.2.1.6) | protein | 89 | 31% helix, 34% strand | P0ADF8 |
| A | Acetolactate synthase isozyme 1 large subunit (EC 2.2.1.6) | protein | 531 | 40% helix, 18% strand | P08142 |
| F | Acetolactate synthase isozyme 1 small subunit (EC 2.2.1.6) | protein | 89 | 33% helix, 33% strand | P0ADF8 |
| B | Acetolactate synthase isozyme 1 large subunit (EC 2.2.1.6) | protein | 539 | 40% helix, 17% strand | P08142 |
| G, H | Acetolactate synthase isozyme 1 small subunit (EC 2.2.1.6) | protein | 88 | 31% helix, 33% strand | P0ADF8 |
| C | Acetolactate synthase isozyme 1 large subunit (EC 2.2.1.6) | protein | 533 | 41% helix, 18% strand | P08142 |
| D | Acetolactate synthase isozyme 1 large subunit (EC 2.2.1.6) | protein | 529 | 41% helix, 17% strand | P08142 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 4 copies · chains A, C, B, D
- TPP · Thiamine diphosphate · ligand · 4 copies · chains A, C, B, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 924 | 0.89 | 0.91 | 120 | FAD, TPP, MG |
| 2 | 953 | 0.88 | 0.89 | 126 | FAD, TPP, MG |
| 3 | 1013 | 0.87 | 0.88 | 119 | FAD, TPP, MG |
| 4 | 567 | 0.86 | 0.92 | 92 | FAD, TPP, MG |
| 5 | 473 | 0.85 | 0.92 | 95 | empty |
Interfaces
16 interfaces between chains.
- B–D · 3186 Ų buried · 24 hydrogen bonds · protein-protein
- A–C · 3021 Ų buried · 24 hydrogen bonds · protein-protein
- F–H · 1202 Ų buried · 10 hydrogen bonds · protein-protein
- E–G · 1151 Ų buried · 5 hydrogen bonds · protein-protein
- H–D · 652 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
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 P0ADF8
- Every structure of UniProt P08142
- Elsewhere: RCSB PDB 6LPI · PDBe 6LPI · UniProt P0ADF8 · UniProt P08142
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