Research workbench
Solution structure of RING-finger in the catalytic subunit (IRX3) of cellulose synthase
Analyse Solution structure of RING-finger in the catalytic subunit (IRX3) of cellulose… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WEO
- Type
- protein
- Length
- 93 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- NOT
- Source
- Arabidopsis thaliana
- Molecule
- cellulose synthase, catalytic subunit (IRX3)
- UniProt
- Q9SWW6
- Ligands
- ZN
Structure
solution nmr · resolution NOT · 1 distinct chain · 10% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | cellulose synthase, catalytic subunit (IRX3) | protein | 93 | 10% helix, 4% strand | Q9SWW6 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1WEO · Solution structure of ring-finger in the catalytic subunit (IRX3) of cellulose synthase · the same entry in another collection · chain A against A, TM-score 1.00
- Q9SWW6 · AlphaFold monomer V2.0 prediction for cellulose synthase a catalytic subunit 7… · a predicted model of the same protein · chain A against A, TM-score 0.64
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 Q9SWW6
- Elsewhere: RCSB PDB 1WEO · PDBe 1WEO · UniProt Q9SWW6
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