Research workbench
Structure of the complex between btub and colicin E2 receptor binding domain
Analyse Structure of the complex between btub and colicin E2 receptor binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2YSU
- Type
- protein
- Length
- 699 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vitamin B12 transporter btub; Colicin-E2
- EC
- 3.1.-.-
- UniProt
- P06129, P04419
- Pockets
- 9 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vitamin B12 transporter btub | protein | 576 | 6% helix, 58% strand | P06129 |
| B | Colicin-E2 (EC 3.1.-.-) | protein | 123 | 85% helix, 0% strand | P04419 |
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 875 | 0.86 | 0.89 | 115 | empty |
| 2 | 1079 | 0.84 | 0.85 | 87 | empty |
| 3 | 176 | 0.81 | 0.97 | 47 | empty |
| 4 | 400 | 0.75 | 0.85 | 49 | empty |
| 5 | 422 | 0.68 | 0.80 | 53 | empty |
Interfaces
1 interface between chains.
- A–B · 1337 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 2YSU · Structure of the complex between BtuB and Colicin E2 receptor binding domain · the same entry in another collection · chain A against A, TM-score 1.00
- P06129 · AlphaFold monomer V2.0 prediction for vitamin B12 transporter btub (P06129) · a predicted model of the same protein · chain A against A, TM-score 0.99
- P04419 · AlphaFold monomer V2.0 prediction for colicin-E2 (P04419) · a predicted model of the same protein · chain B against A, TM-score 0.95
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 P06129
- Every structure of UniProt P04419
- Elsewhere: RCSB PDB 2YSU · PDBe 2YSU · UniProt P06129 · UniProt P04419
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