Research workbench
The structure of arabidopsis CLPT1
Analyse The structure of arabidopsis CLPT1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Y0B
- Type
- protein
- Length
- 278 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Double clp-N motif protein
- UniProt
- Q93WL3
- Ligands
- CL
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 62% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Double clp-N motif protein | protein | 140 | 61% helix, 3% strand | Q93WL3 |
| B | Double clp-N motif protein | protein | 138 | 62% helix, 3% strand | Q93WL3 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 296 | 0.55 | 0.76 | 43 | CL |
Interfaces
1 interface between chains.
- A–B · 260 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 modified (engineered).
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 Q93WL3
- Elsewhere: RCSB PDB 4Y0B · PDBe 4Y0B · UniProt Q93WL3
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