Research workbench
Pyochelin outer membrane receptor fpta from pseudomonas aeruginosa
Analyse Pyochelin outer membrane receptor fpta 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
- 1XKW
- Type
- protein
- Length
- 655 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- FE(III)-pyochelin receptor
- UniProt
- P42512
- Ligands
- 188, SO4
- Pockets
- 7 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 61% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | FE(III)-pyochelin receptor | protein | 655 | 3% helix, 61% strand | P42512 |
Ligands and binding sites
- 188 · Pyochelin fe(iii) · ligand · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
- LDA · Lauryl dimethylamine-N-oxide · additive · 5 copies · chains A
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 593 | 0.88 | 0.93 | 86 | empty |
| 2 | 504 | 0.71 | 0.81 | 61 | empty |
| 3 | 296 | 0.69 | 0.84 | 46 | empty |
| 4 | 507 | 0.68 | 0.79 | 63 | empty |
| 5 | 65 | 0.61 | 0.90 | 21 | empty |
Compared structures
- 1XKW · Pyochelin outer membrane receptor FptA from Pseudomonas aeruginosa · the same entry in another collection · chain A against A, TM-score 1.00
- P42512 · AlphaFold monomer V2.0 prediction for FE(3+)-pyochelin receptor (P42512) · 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 P42512
- Elsewhere: RCSB PDB 1XKW · PDBe 1XKW · UniProt P42512
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