MolNFT v2 · #220124 · protein
Crystal Structure of Bacterioferritin (Bfr) from Brucella abortus (Apo, F16L mutant)
8SQP: “Crystal Structure of Bacterioferritin (Bfr) from Brucella abortus (Apo, F16L mutant)”. X-ray diffraction at 2.05, 3 ligands (HEM, CA, CL), 1 pocket (best druggability 0.50). MolNFT v2 #220124 on GenesisL1: 3D structure, binding…
- PDB
- 8SQP
- Type
- protein
- Length
- 158 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.05
- Source
- Brucella abortus 2308
- Molecule
- Bacterioferritin
- EC
- 1.16.3.1
- UniProt
- Q2YKI4
- Ligands
- HEM, CA, CL
- Pockets
- 1 · best druggability 0.50
Structure
x-ray diffraction · resolution 2.05 · 1 distinct chain · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bacterioferritin (EC 1.16.3.1) | protein | 158 | 79% helix, 0% strand | Q2YKI4 |
Ligands and binding sites
- HEM · Protoporphyrin IX containing Fe · ligand · chains A
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · 3 copies · 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 | 90 | 0.50 | 0.83 | 20 | empty |
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 Q2YKI4
- Elsewhere: RCSB PDB 8SQP · PDBe 8SQP · UniProt Q2YKI4
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