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Crystal structure of complement factor D mutant R202A
Analyse Crystal structure of complement factor D mutant R202A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XWA
- Type
- protein
- Length
- 456 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement factor D
- EC
- 3.4.21.46
- UniProt
- P00746
- Pockets
- 6 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Complement factor D (EC 3.4.21.46) | protein | 228 | 8% helix, 36% strand | P00746 |
Ligands and binding sites
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 693 | 0.69 | 0.77 | 58 | empty |
| 2 | 62 | 0.41 | 0.81 | 15 | empty |
| 3 | 53 | 0.37 | 0.80 | 18 | empty |
| 4 | 84 | 0.36 | 0.76 | 20 | empty |
| 5 | 88 | 0.34 | 0.74 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 510 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 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 2XWA · PDBe 2XWA · UniProt P00746
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