MolNFT v2 · #150172 · protein
Complement factor D in complex with the inhibitor (4-((3-(aminomethyl)phenyl)amino)quinazolin-2-yl)-L-valine
6FUH: “Complement factor D in complex with the inhibitor (4-((3-(aminomethyl)phenyl)amino)quinazolin-2-yl)-L-valine”. X-ray diffraction at 1.37, 1 ligand (E88), 1 pocket (best druggability 0.49). MolNFT v2 #150172 on GenesisL1: 3D…
- PDB
- 6FUH
- Type
- protein
- Length
- 228 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.37
- Source
- Homo sapiens
- Molecule
- Complement factor D
- EC
- 3.4.21.46
- UniProt
- P00746
- Ligands
- E88
- Pockets
- 1 · best druggability 0.49
Structure
x-ray diffraction · resolution 1.37 · 1 distinct chain · 9% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement factor D (EC 3.4.21.46) | protein | 228 | 9% helix, 36% strand | P00746 |
Ligands and binding sites
- E88 · (2~{S})-2-[[4-[[3-(aminomethyl)phenyl]amino]quinazolin-2-yl]amino]-3-methyl-butanoic acid · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 130 | 0.49 | 0.79 | 29 | E88 |
Modifications
Observed in the structure: 4 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 P00746
- Elsewhere: RCSB PDB 6FUH · PDBe 6FUH · UniProt P00746
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