Research workbench
Elastase of pseudomonas aeruginosa with an inhibitor
Analyse Elastase of pseudomonas aeruginosa with an inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1U4G
- Type
- protein
- Length
- 298 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elastase
- EC
- 3.4.24.26
- UniProt
- P14756
- Ligands
- HPI, ZN, CA, SO4
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elastase (EC 3.4.24.26) | protein | 298 | 41% helix, 15% strand | P14756 |
Ligands and binding sites
- HPI · N-(1-carboxy-3-phenylpropyl)phenylalanyl-alpha-asparagine · ligand · chains A
- ZN · Zinc ion · metal · chains A
- CA · Calcium ion · metal · chains A
- SO4 · Sulfate ion · ion · 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 | 125 | 0.52 | 0.81 | 28 | HPI |
| 2 | 53 | 0.49 | 0.86 | 20 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 P14756
- Elsewhere: RCSB PDB 1U4G · PDBe 1U4G · UniProt P14756
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