Research workbench
Crystal Structure of Recombinant Human Complement Protein C8gamma
Analyse Crystal Structure of Recombinant Human Complement Protein C8gamma in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2OVE
- Type
- protein
- Length
- 162 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Homo sapiens
- Molecule
- Complement component 8, gamma polypeptide
- UniProt
- Q14CU0
- Pockets
- 1 · best druggability 0.58
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 17% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement component 8, gamma polypeptide | protein | 162 | 17% helix, 46% strand | Q14CU0 |
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 | 271 | 0.58 | 0.77 | 28 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2OVE · Crystal structure of recombinant human complement protein C8GAMMA · 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 Q14CU0
- Elsewhere: RCSB PDB 2OVE · PDBe 2OVE · UniProt Q14CU0
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