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Crystal structure of HET-C2: A FUNGAL GLYCOLIPID TRANSFER PROTEIN (GLTP)
Analyse Crystal structure of HET-C2: A FUNGAL GLYCOLIPID TRANSFER PROTEIN (GLTP) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3KV0
- Type
- protein
- Length
- 194 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.9
- Source
- Podospora anserina
- Molecule
- Het-C2
- UniProt
- Q01494
- Pockets
- 1 · best druggability 0.37
Structure
x-ray diffraction · resolution 1.9 · 1 distinct chain · 75% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Het-C2 | protein | 194 | 75% helix, 3% strand | Q01494 |
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 | 81 | 0.37 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 17 modified (methylation).
Compared structures
- 3KV0 · Crystal structure of het-C2: a fungal glycolipid transfer protein (gltp) · 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 Q01494
- Elsewhere: RCSB PDB 3KV0 · PDBe 3KV0 · UniProt Q01494
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