Research workbench
Crystal structure of aeromonas proteolytica aminopeptidase complexed with 8-quinolinol
Analyse Crystal structure of aeromonas proteolytica aminopeptidase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VH9
- Type
- protein
- Length
- 291 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacterial leucyl aminopeptidase
- EC
- 3.4.11.10
- UniProt
- Q01693
- Ligands
- HQY, NA, ZN, CL, SCN
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bacterial leucyl aminopeptidase (EC 3.4.11.10) | protein | 291 | 41% helix, 19% strand | Q01693 |
Ligands and binding sites
- HQY · quinolin-8-ol · ligand · chains A
- NA · Sodium ion · metal · 9 copies · chains A
- ZN · Zinc ion · metal · 2 copies · chains A
- CL · Chloride ion · ion · 9 copies · chains A
- SCN · Thiocyanate ion · ion · 2 copies · chains A
- GOL · Glycerol · additive · 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, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 56 | 0.43 | 0.83 | 18 | HQY, NA |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3VH9 · Crystal structure of Aeromonas proteolytica aminopeptidase complexed with 8-quinolinol · the same entry in another collection · chain A against A, TM-score 1.00
- Q01693 · AlphaFold monomer V2.0 prediction for bacterial leucyl aminopeptidase (Q01693) · 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 Q01693
- Elsewhere: RCSB PDB 3VH9 · PDBe 3VH9 · UniProt Q01693
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