MolNFT v1 · #177397 · protein
Acetolactate synthase from trichoderma harzianum
7EHE: “Acetolactate synthase from trichoderma harzianum”. X-ray diffraction, 3 ligands (FAD, TZD, MG). MolNFT v1 #177397 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7EHE
- Type
- protein
- Length
- 1,170 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A2N1LPC4
- Ligands
- FAD, TZD, MG
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 589 | — | A0A2N1LPC4 |
| B | — | protein | 581 | — | A0A2N1LPC4 |
Ligands and binding sites
- FAD · Flavin-adenine dinucleotide · ligand · 2 copies · chains A, B
- TZD · 2-{3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-2-oxo-2,3-dihydro-1,3-thiazol-5-yl}ethyl trihydrogen diphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7EHE · Acetolactate Synthase from Trichoderma harzianum · 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 A0A2N1LPC4
- Elsewhere: RCSB PDB 7EHE · PDBe 7EHE · UniProt A0A2N1LPC4
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