Research workbench
Chimeric Rat C5a
Analyse Chimeric Rat C5a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6JV7
- Type
- protein
- Length
- 154 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.309
- Molecule
- Chimeric-rC5a; D-anaphylatoxin C5a
- UniProt
- P08650
- Ligands
- SO4
Structure
x-ray diffraction · resolution 1.309 · 2 distinct chains · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chimeric-rC5a | protein | 77 | 64% helix, 0% strand | P08650 |
| B | D-anaphylatoxin C5a | protein | 77 | 62% helix, 0% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 529 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 73 d-amino, 6 disulfide, 3 modified (D-amino acid, disulfide, nonstandard).
Compared structures
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 P08650
- Elsewhere: RCSB PDB 6JV7 · PDBe 6JV7 · UniProt P08650
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