Research workbench
Outer membrane cobalamin transporter (btub) from E. COLI
Analyse Outer membrane cobalamin transporter (btub) from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NQE
- Type
- protein
- Length
- 549 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vitamin B12 receptor
- UniProt
- P06129
- Ligands
- MG
- Pockets
- 7 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 62% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vitamin B12 receptor | protein | 549 | 7% helix, 62% strand | P06129 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
- C8E · (hydroxyethyloxy)tri(ethyloxy)octane · additive · 7 copies · 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 | 768 | 0.86 | 0.90 | 100 | empty |
| 2 | 132 | 0.78 | 0.96 | 38 | empty |
| 3 | 76 | 0.74 | 0.98 | 33 | empty |
| 4 | 400 | 0.70 | 0.82 | 40 | empty |
| 5 | 509 | 0.69 | 0.79 | 49 | empty |
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 P06129
- Elsewhere: RCSB PDB 1NQE · PDBe 1NQE · UniProt P06129
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