Research workbench
M-ficolin mutant Y271F
Analyse M-ficolin mutant Y271F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2WNP
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.21
- Source
- HOMO SAPIENS
- Molecule
- Ficolin-1
- UniProt
- O00602
- Ligands
- CA
Structure
x-ray diffraction · resolution 1.21 · 1 distinct chain · 16% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| F | Ficolin-1 | protein | 217 | 16% helix, 32% strand | O00602 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 O00602
- Elsewhere: RCSB PDB 2WNP · PDBe 2WNP · UniProt O00602
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