Research workbench
Crystal structure of the coiled-coil domain of the transient receptor potential channel from gibberella zeae (trpgz)
Analyse Crystal structure of the coiled-coil domain of the transient receptor potential… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3VVI
- Type
- protein
- Length
- 168 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Non selective cation channel homologous to TRP channel
- UniProt
- I1RJZ4
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Non selective cation channel homologous to TRP channel | protein | 21 | 81% helix, 0% strand | I1RJZ4 |
Ligands and binding sites
- ACT · Acetate ion · additive · 3 copies · chains C, B, F, H
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 | 234 | 0.49 | 0.75 | 37 | ACT |
Interfaces
13 interfaces between chains.
- F–G · 536 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 527 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 491 Ų buried · 5 hydrogen bonds · protein-protein
- E–F · 491 Ų buried · 4 hydrogen bonds · protein-protein
- C–D · 452 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 3VVI · Crystal structure of the coiled-coil domain of the transient receptor potential channel… · 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 I1RJZ4
- Elsewhere: RCSB PDB 3VVI · PDBe 3VVI · UniProt I1RJZ4
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