Research workbench
Impa metallopeptidase from pseudomonas aeruginosa
Analyse Impa metallopeptidase from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5KDV
- Type
- protein
- Length
- 891 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metallopeptidase
- UniProt
- Q9I5W4
- Ligands
- ZN, SO4
- Pockets
- 6 · best druggability 0.66
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metallopeptidase | protein | 891 | 40% helix, 15% strand | Q9I5W4 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
- EDO · 1,2-ethanediol · additive · 25 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 414 | 0.66 | 0.79 | 56 | empty |
| 2 | 358 | 0.61 | 0.77 | 47 | EDO |
| 3 | 167 | 0.52 | 0.79 | 25 | EDO |
| 4 | 104 | 0.43 | 0.77 | 16 | empty |
| 5 | 104 | 0.37 | 0.75 | 21 | EDO |
Modifications
Observed in the structure: 4 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 Q9I5W4
- Elsewhere: RCSB PDB 5KDV · PDBe 5KDV · UniProt Q9I5W4
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