Research workbench
Leucine aminopeptidase complex with L-leucinal
Analyse Leucine aminopeptidase complex with L-leucinal in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LAN
- Type
- protein
- Length
- 484 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Bos taurus
- Molecule
- Leucine aminopeptidase
- EC
- 3.4.11.1
- UniProt
- P00727
- Ligands
- LEU, ZN
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · resolution 1.9 · 1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Leucine aminopeptidase (EC 3.4.11.1) | protein | 484 | 39% helix, 22% strand | P00727 |
Ligands and binding sites
- LEU · Leucine · ligand · chains A
- ZN · Zinc ion · metal · 3 copies · chains A
- MRD · (4R)-2-methylpentane-2,4-diol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 247 | 0.50 | 0.75 | 39 | LEU |
| 2 | 187 | 0.47 | 0.75 | 30 | empty |
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 P00727
- Elsewhere: RCSB PDB 1LAN · PDBe 1LAN · UniProt P00727
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