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Crystal structure of GH62 hydrolase from thermophilic fungus Scytalidium thermophilum
Analyse Crystal structure of GH62 hydrolase from thermophilic fungus Scytalidium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4PVA
- Type
- protein
- Length
- 328 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.23
- Source
- Scytalidium thermophilum
- Molecule
- GH62 hydrolase
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.48
Structure
x-ray diffraction · resolution 1.23 · 1 distinct chain · 9% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | GH62 hydrolase | protein | 328 | 9% helix, 42% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 130 | 0.48 | 0.79 | 20 | PO4 |
| 2 | 63 | 0.45 | 0.82 | 15 | empty |
| 3 | 80 | 0.35 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 4PVA · Crystal structure of GH62 hydrolase from thermophilic fungus scytalidium thermophilum · 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
- Elsewhere: RCSB PDB 4PVA · PDBe 4PVA
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