Research workbench
VLM2 thioesterase domain wild type structure 1
Analyse VLM2 thioesterase domain wild type structure 1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ECB
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- VLM2
- EC
- 3.1.2.-
- UniProt
- Q1PSF3
- Pockets
- 2 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | VLM2 (EC 3.1.2.-) | protein | 263 | 43% helix, 14% strand | Q1PSF3 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 447 | 0.70 | 0.81 | 49 | empty |
| 2 | 70 | 0.31 | 0.74 | 20 | empty |
Compared structures
- 6ECB · Vlm2 thioesterase domain wild type structure 1 · 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 Q1PSF3
- Elsewhere: RCSB PDB 6ECB · PDBe 6ECB · UniProt Q1PSF3
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