Research workbench
The periplasmic binding protein ceue of campylobacter jejuni binds the IRON(III) complex of azotochelin
Analyse The periplasmic binding protein ceue of campylobacter jejuni binds the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OAH
- Type
- protein
- Length
- 864 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enterochelin ABC transporter substrate-binding protein
- UniProt
- A0A1E7P069
- Ligands
- 95B, FE
- Pockets
- 5 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Enterochelin ABC transporter substrate-binding protein | protein | 288 | 42% helix, 20% strand | A0A1E7P069 |
Ligands and binding sites
- 95B · Azotochelin · ligand · 2 copies · chains A, B
- FE · Fe (III) ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 974 | 0.78 | 0.80 | 113 | empty |
| 2 | 432 | 0.63 | 0.77 | 30 | empty |
| 3 | 236 | 0.63 | 0.82 | 35 | empty |
| 4 | 307 | 0.63 | 0.80 | 37 | empty |
| 5 | 361 | 0.55 | 0.74 | 43 | empty |
Interfaces
3 interfaces between chains.
- A–C · 540 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 460 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 360 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 5OAH · THE PERIPLASMIC BINDING PROTEIN CEUE OF CAMPYLOBACTER JEJUNI BINDS THE IRON(III) COMPLEX… · the same entry in another collection · chain B against B, 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 A0A1E7P069
- Elsewhere: RCSB PDB 5OAH · PDBe 5OAH · UniProt A0A1E7P069
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