Research workbench
Crystal structure of udp-glucose 4-epimerase
Analyse Crystal structure of udp-glucose 4-epimerase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2C20
- Type
- protein
- Length
- 1,974 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-glucose 4-epimerase
- EC
- 5.1.3.2
- UniProt
- Q81K34
- Ligands
- NAD, ZN
- Pockets
- 13 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Udp-glucose 4-epimerase (EC 5.1.3.2) | protein | 329 | 40% helix, 17% strand | Q81K34 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 6 copies · chains A, B, C, D, E, F
- ZN · Zinc ion · metal · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 843 | 0.80 | 0.83 | 84 | NAD |
| 2 | 755 | 0.79 | 0.83 | 80 | NAD |
| 3 | 861 | 0.79 | 0.82 | 73 | NAD |
| 4 | 861 | 0.79 | 0.82 | 75 | NAD |
| 5 | 874 | 0.79 | 0.82 | 75 | NAD |
Interfaces
3 interfaces between chains.
- E–F · 1081 Ų buried · 8 hydrogen bonds · protein-protein
- C–D · 1070 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 1043 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 2C20 · Crystal structure of udp-glucose 4-epimerase · the same entry in another collection · chain A against A, 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 Q81K34
- Elsewhere: RCSB PDB 2C20 · PDBe 2C20 · UniProt Q81K34
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