Research workbench
Crystal structure of bacterial fucu
Analyse Crystal structure of bacterial fucu in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WCV
- Type
- protein
- Length
- 1,395 residues
- Chains
- 10
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-fucose mutarotase
- EC
- 5.1.3.-
- UniProt
- A8A3T9
- Ligands
- FUC
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 4 distinct chains · 28% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-fucose mutarotase (EC 5.1.3.-) | protein | 138 | 28% helix, 20% strand | A8A3T9 |
| B, D, F, G, H, I, J | L-fucose mutarotase (EC 5.1.3.-) | protein | 140 | 29% helix, 20% strand | A8A3T9 |
| C | L-fucose mutarotase (EC 5.1.3.-) | protein | 138 | 28% helix, 20% strand | A8A3T9 |
| E | L-fucose mutarotase (EC 5.1.3.-) | protein | 139 | 28% helix, 22% strand | A8A3T9 |
Ligands and binding sites
- FUC · alpha-L-fucopyranose · sugar · 10 copies · chains A, E, B, C, D, F, J, G, H, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 751 | 0.77 | 0.81 | 76 | FUC |
| 2 | 940 | 0.75 | 0.78 | 48 | empty |
| 3 | 1122 | 0.73 | 0.76 | 86 | empty |
| 4 | 645 | 0.71 | 0.79 | 54 | empty |
| 5 | 55 | 0.70 | 0.97 | 14 | FUC |
Interfaces
20 interfaces between chains.
- E–H · 569 Ų buried · 5 hydrogen bonds · protein-protein
- B–J · 519 Ų buried · 3 hydrogen bonds · protein-protein
- C–D · 494 Ų buried · 7 hydrogen bonds · protein-protein
- G–H · 491 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 490 Ų buried · 7 hydrogen bonds · protein-protein
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 A8A3T9
- Elsewhere: RCSB PDB 2WCV · PDBe 2WCV · UniProt A8A3T9
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