Research workbench
Crystal structure of the ferric enterobactin receptor (pfea) from pseudomonas aeruginosa
Analyse Crystal structure of the ferric enterobactin receptor (pfea) from pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5M9B
- Type
- protein
- Length
- 707 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferric enterobactin receptor
- UniProt
- Q05098
- Pockets
- 10 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ferric enterobactin receptor | protein | 707 | 7% helix, 52% strand | Q05098 |
Ligands and binding sites
- ACY · Acetic acid · additive · 6 copies · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 321 | 0.85 | 0.95 | 65 | EDO |
| 2 | 415 | 0.85 | 0.93 | 46 | ACY |
| 3 | 530 | 0.79 | 0.86 | 73 | ACY |
| 4 | 479 | 0.69 | 0.80 | 40 | ACY, EDO |
| 5 | 50 | 0.65 | 0.96 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5M9B · Crystal structure of the ferric enterobactin receptor (PfeA) from Pseudomonas aeruginosa · the same entry in another collection · chain A against A, TM-score 1.00
- Q05098 · AlphaFold monomer V2.0 prediction for ferric enterobactin receptor (Q05098) · 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 Q05098
- Elsewhere: RCSB PDB 5M9B · PDBe 5M9B · UniProt Q05098
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