Research workbench
Pseudomonas aeruginosa exotoxin a, P201Q, W281A mutant
Analyse Pseudomonas aeruginosa exotoxin a, P201Q, W281A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1IKP
- Type
- protein
- Length
- 599 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Exotoxin a
- EC
- 2.4.2.-
- UniProt
- P11439
- Ligands
- NA, CL
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Exotoxin a (EC 2.4.2.-) | protein | 599 | 30% helix, 26% strand | P11439 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 660 | 0.76 | 0.82 | 70 | empty |
| 2 | 354 | 0.66 | 0.80 | 36 | empty |
| 3 | 358 | 0.64 | 0.79 | 48 | empty |
| 4 | 124 | 0.58 | 0.84 | 34 | empty |
| 5 | 178 | 0.53 | 0.79 | 37 | empty |
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 P11439
- Elsewhere: RCSB PDB 1IKP · PDBe 1IKP · UniProt P11439
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