Research workbench
Crystal structure of TEX12 F102A F109E V116A in an alternative conformation
Analyse Crystal structure of TEX12 F102A F109E V116A in an alternative conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6R2F
- Type
- protein
- Length
- 245 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Testis-expressed protein 12
- UniProt
- Q9BXU0
- Ligands
- CL
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · 3 distinct chains · 95% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Testis-expressed protein 12 | protein | 64 | 92% helix, 0% strand | Q9BXU0 |
| C | Testis-expressed protein 12 | protein | 58 | 97% helix, 0% strand | Q9BXU0 |
| D | Testis-expressed protein 12 | protein | 59 | 97% helix, 0% strand | Q9BXU0 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, D
- MPD · (4S)-2-methyl-2,4-pentanediol · additive · 11 copies · chains A, B, D, C
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 | 341 | 0.67 | 0.81 | 30 | MPD, CL |
Interfaces
5 interfaces between chains.
- A–B · 1486 Ų buried · 13 hydrogen bonds · protein-protein
- C–D · 1275 Ų buried · 5 hydrogen bonds · protein-protein
- B–C · 392 Ų buried · 0 hydrogen bonds · protein-protein
- A–D · 375 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 243 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6R2F · Crystal structure of TEX12 F102A F109E V116A in an alternative conformation · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BXU0 · AlphaFold monomer V2.0 prediction for testis-expressed protein 12 (Q9BXU0) · a predicted model of the same protein · chain D against A, TM-score 0.96
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 Q9BXU0
- Elsewhere: RCSB PDB 6R2F · PDBe 6R2F · UniProt Q9BXU0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.