Research workbench
The crystal structure of bovine lens leucine aminopeptidase in complex with zofenoprilat
Analyse The crystal structure of bovine lens leucine aminopeptidase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EWB
- Type
- protein
- Length
- 486 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytosol aminopeptidase
- EC
- 3.4.11.1
- UniProt
- P00727
- Ligands
- ZED, ZN, NA, CO3
- Pockets
- 3 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytosol aminopeptidase (EC 3.4.11.1) | protein | 486 | 39% helix, 22% strand | P00727 |
Ligands and binding sites
- ZED · L-proline, 1-[(2S)-3-mercapto-2-methyl-1-oxopropyl]-4-(phenylthio)-, 4S · ligand · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- NA · Sodium ion · metal · chains A
- CO3 · Carbonate ion · ion · chains A
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 248 | 0.50 | 0.75 | 36 | CO3, ZED |
| 2 | 138 | 0.42 | 0.75 | 19 | empty |
| 3 | 66 | 0.33 | 0.76 | 18 | empty |
Compared structures
- 2EWB · The crystal structure of Bovine Lens Leucine Aminopeptidase in complex with zofenoprilat · 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 2EWB · PDBe 2EWB · UniProt P00727
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