Research workbench
The crystal structure of cpftsy from arabidopsis thaliana
Analyse The crystal structure of cpftsy from arabidopsis thaliana in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3B9Q
- Type
- protein
- Length
- 298 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chloroplast srp receptor homolog, alpha subunit cpftsy
- UniProt
- Q9SWS7
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chloroplast srp receptor homolog, alpha subunit cpftsy | protein | 298 | 55% helix, 12% strand | Q9SWS7 |
Ligands and binding sites
- MLI · Malonate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 88 | 0.33 | 0.74 | 20 | empty |
Compared structures
- 3B9Q · The crystal structure of cpFtsY from Arabidopsis thaliana · 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 Q9SWS7
- Elsewhere: RCSB PDB 3B9Q · PDBe 3B9Q · UniProt Q9SWS7
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