Research workbench
L-alanine dehydrogenase complexed with pyruvate
Analyse L-alanine dehydrogenase complexed with pyruvate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1SAY
- Type
- protein
- Length
- 361 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-alanine dehydrogenase
- EC
- 1.4.1.1
- UniProt
- O52942
- Ligands
- PYR
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-alanine dehydrogenase (EC 1.4.1.1) | protein | 361 | 40% helix, 18% strand | O52942 |
Ligands and binding sites
- PYR · Pyruvic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 699 | 0.71 | 0.78 | 69 | PYR |
Compared structures
- 1SAY · L-alanine dehydrogenase complexed with pyruvate · 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 O52942
- Elsewhere: RCSB PDB 1SAY · PDBe 1SAY · UniProt O52942
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