MolNFT v1 · #20838 · protein
Crystal structure analysis of the bb segment of factor B
1RRK · Complement factor B: “Crystal structure analysis of the bb segment of factor B”. X-ray diffraction, 3 ligands (NA, CO, IOD), 5 pockets (best druggability 0.52). MolNFT v1 #20838 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1RRK
- Type
- protein
- Length
- 480 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
- NA, CO, IOD
- Pockets
- 5 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Complement factor B (EC 3.4.21.47) | protein | 480 | 29% helix, 26% strand | P00751 |
Ligands and binding sites
- NA · Sodium ion · metal · 7 copies · chains A
- CO · Cobalt (II) ion · metal · chains A
- IOD · Iodide ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 170 | 0.52 | 0.78 | 25 | empty |
| 2 | 188 | 0.52 | 0.78 | 40 | empty |
| 3 | 87 | 0.50 | 0.83 | 20 | empty |
| 4 | 92 | 0.45 | 0.80 | 22 | empty |
| 5 | 50 | 0.29 | 0.75 | 12 | empty |
Modifications
Observed in the structure: 6 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 P00751
- Elsewhere: RCSB PDB 1RRK · PDBe 1RRK · UniProt P00751
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