Research workbench
Bovine lens leucine aminopeptidase complexed with L-leucine phosphonic acid
Analyse Bovine lens leucine aminopeptidase complexed with L-leucine phosphonic acid in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LCP
- Type
- protein
- Length
- 968 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Leucine aminopeptidase
- EC
- 3.4.11.1
- UniProt
- P00727
- Ligands
- PLU, ZN
- Pockets
- 8 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Leucine aminopeptidase (EC 3.4.11.1) | protein | 484 | 39% helix, 21% strand | P00727 |
Ligands and binding sites
- PLU · Leucine phosphonic acid · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 6 copies · chains A, B
- MRD · (4R)-2-methylpentane-2,4-diol · additive · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 465 | 0.62 | 0.76 | 50 | PLU |
| 2 | 381 | 0.60 | 0.76 | 49 | PLU |
| 3 | 251 | 0.58 | 0.78 | 31 | empty |
| 4 | 185 | 0.57 | 0.81 | 35 | MRD |
| 5 | 209 | 0.56 | 0.79 | 33 | MRD |
Interfaces
1 interface between chains.
- A–B · 1587 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 1LCP · Bovine lens leucine aminopeptidase complexed with L-leucine phosphonic acid · the same entry in another collection · chain A against A, TM-score 1.00
- P00727 · AlphaFold monomer V2.0 prediction for cytosol aminopeptidase (P00727) · a predicted model of the same protein · 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 P00727
- Elsewhere: RCSB PDB 1LCP · PDBe 1LCP · UniProt P00727
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