MolNFT v1 · #46956 · protein
Human complement factor B
2OK5: “Human complement factor B”. X-ray diffraction, 3 ligands (NAG, MAN, BMA), 10 pockets (best druggability 0.82). MolNFT v1 #46956 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2OK5
- Type
- protein
- Length
- 710 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Complement factor B
- EC
- 3.4.21.47
- UniProt
- P00751
- Ligands
- NAG, MAN, BMA
- Pockets
- 10 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement factor B (EC 3.4.21.47) | protein | 710 | 20% helix, 29% strand | P00751 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A
- MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A
- BMA · beta-D-mannopyranose · sugar
- GOL · Glycerol · additive · 13 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 875 | 0.82 | 0.84 | 81 | GOL |
| 2 | 547 | 0.79 | 0.86 | 53 | empty |
| 3 | 187 | 0.49 | 0.77 | 27 | empty |
| 4 | 99 | 0.47 | 0.80 | 22 | empty |
| 5 | 189 | 0.46 | 0.75 | 22 | empty |
Modifications
Observed in the structure: 11 disulfide, 4 glycan (disulfide, N-glycosylation).
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 P00751
- Elsewhere: RCSB PDB 2OK5 · PDBe 2OK5 · UniProt P00751
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.