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Acetolactate synthase from bacillus subtilis bound to thdp - crystal form I
Analyse Acetolactate synthase from bacillus subtilis bound to thdp - crystal form I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4RJI
- Type
- protein
- Length
- 2,201 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetolactate synthase
- EC
- 4.1.3.18
- UniProt
- V5MX36
- Ligands
- TPP, MG
- Pockets
- 20 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 43% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetolactate synthase (EC 4.1.3.18) | protein | 539 | 43% helix, 17% strand | V5MX36 |
| B | Acetolactate synthase (EC 4.1.3.18) | protein | 552 | 43% helix, 17% strand | V5MX36 |
| C, D | Acetolactate synthase (EC 4.1.3.18) | protein | 555 | 45% helix, 17% strand | V5MX36 |
Ligands and binding sites
- TPP · Thiamine diphosphate · ligand · 4 copies · chains A, B, C, D
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
- PG4 · Tetraethylene glycol · additive · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 513 | 0.78 | 0.86 | 68 | empty |
| 2 | 470 | 0.78 | 0.85 | 54 | TPP, MG |
| 3 | 452 | 0.78 | 0.86 | 54 | TPP |
| 4 | 370 | 0.77 | 0.87 | 61 | empty |
| 5 | 444 | 0.76 | 0.85 | 55 | TPP, MG |
Interfaces
6 interfaces between chains.
- A–B · 3659 Ų buried · 74 hydrogen bonds · protein-protein
- C–D · 3651 Ų buried · 80 hydrogen bonds · protein-protein
- A–D · 1374 Ų buried · 26 hydrogen bonds · protein-protein
- B–C · 1368 Ų buried · 29 hydrogen bonds · protein-protein
- B–D · 639 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 4RJI · Acetolactate synthase from Bacillus subtilis bound to ThDP - crystal form I · the same entry in another collection · chain B against B, 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 V5MX36
- Elsewhere: RCSB PDB 4RJI · PDBe 4RJI · UniProt V5MX36
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