MolNFT v1 · #62500 · protein
Crystal structure of udp-glucose 4 epimerase (gale-1) from archaeoglobus fulgidus
3EHE · Udp-glucose 4-epimerase (gale-1): “Crystal structure of udp-glucose 4 epimerase (gale-1) from archaeoglobus fulgidus”. X-ray diffraction, 1 ligand (NAD), 6 pockets (best druggability 0.76). MolNFT v1 #62500 on GenesisL1: 3D…
- PDB
- 3EHE
- Type
- protein
- Length
- 580 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Udp-glucose 4-epimerase (gale-1)
- UniProt
- O29886
- Ligands
- NAD
- Pockets
- 6 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Udp-glucose 4-epimerase (gale-1) | protein | 290 | 41% helix, 17% strand | O29886 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 602 | 0.76 | 0.82 | 62 | NAD |
| 2 | 582 | 0.75 | 0.82 | 68 | NAD |
| 3 | 217 | 0.59 | 0.80 | 38 | empty |
| 4 | 138 | 0.39 | 0.73 | 24 | empty |
| 5 | 63 | 0.32 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1219 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 3EHE · Crystal structure of UDP-glucose 4 epimerase (galE-1) from Archaeoglobus fulgidus · 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 O29886
- Elsewhere: RCSB PDB 3EHE · PDBe 3EHE · UniProt O29886
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