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The crystal structure of btum cobalamin transporter
Analyse The crystal structure of btum cobalamin transporter in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FFV
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Btum
- UniProt
- Q3SFD8
- Ligands
- BNG, B12
- Pockets
- 4 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Btum | protein | 194 | 74% helix, 0% strand | Q3SFD8 |
Ligands and binding sites
- BNG · nonyl beta-D-glucopyranoside · ligand · 3 copies · chains A
- B12 · Cobalamin · ligand · chains A
- PEG · Di(hydroxyethyl)ether · additive · 7 copies · chains A
- PG4 · Tetraethylene glycol · additive · 5 copies · chains A
- PGE · Triethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 467 | 0.68 | 0.79 | 37 | B12 |
| 2 | 183 | 0.54 | 0.78 | 19 | BNG |
| 3 | 141 | 0.50 | 0.78 | 27 | PG4 |
| 4 | 51 | 0.28 | 0.74 | 14 | empty |
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 Q3SFD8
- Elsewhere: RCSB PDB 6FFV · PDBe 6FFV · UniProt Q3SFD8
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