Research workbench
Crystallographic structures of ILVN.VAL/ILE COMPLEXES:CONFORMATIONAL selectivity for feedback inhibition of ahass
Analyse Crystallographic structures of ILVN.VAL/ILE COMPLEXES:CONFORMATIONAL… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5YUM
- Type
- protein
- Length
- 91 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetolactate synthase isozyme 1 small subunit
- EC
- 2.2.1.6
- UniProt
- P0ADF8
- Ligands
- ILE, CO
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetolactate synthase isozyme 1 small subunit (EC 2.2.1.6) | protein | 91 | 27% helix, 33% strand | P0ADF8 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5YUM · Crystallographic structures of IlvN.Val/Ile complexes:Conformational selectivity for… · the same entry in another collection · chain A against A, TM-score 1.00
- P0ADF8 · AlphaFold monomer V2.0 prediction for acetolactate synthase isozyme 1 small subunit… · a predicted model of the same protein · chain A against A, TM-score 0.86
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
- Elsewhere: RCSB PDB 5YUM · PDBe 5YUM · UniProt P0ADF8
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