Research workbench
Structural insight into nucleotide rhamnose SYNTHASE/EPIMERASE- reductase from arabidopsis thaliana
Analyse Structural insight into nucleotide rhamnose SYNTHASE/EPIMERASE- reductase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QQR
- Type
- protein
- Length
- 542 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3,5-EPIMERASE/4-reductase
- UniProt
- Q9LQ04
- Ligands
- ZN, CL, SO4
- Pockets
- 4 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3,5-EPIMERASE/4-reductase | protein | 274 | 40% helix, 15% strand | Q9LQ04 |
| B | 3,5-EPIMERASE/4-reductase | protein | 268 | 41% helix, 16% strand | Q9LQ04 |
Ligands and binding sites
- ZN · Zinc ion · metal · 7 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 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 | 374 | 0.61 | 0.77 | 42 | ZN |
| 2 | 144 | 0.59 | 0.84 | 30 | ZN |
| 3 | 191 | 0.48 | 0.75 | 16 | empty |
| 4 | 142 | 0.41 | 0.74 | 34 | SO4 |
Interfaces
1 interface between chains.
- A–B · 1156 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 4QQR · Structural insight into nucleotide rhamnose synthase/epimerase-reductase from Arabidopsis… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9LQ04 · AlphaFold monomer V2.0 prediction for bifunctional dtdp-4-dehydrorhamnose… · a predicted model of the same protein · chain B against A, TM-score 0.98
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 Q9LQ04
- Elsewhere: RCSB PDB 4QQR · PDBe 4QQR · UniProt Q9LQ04
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.