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1.65 a resolution structure of apo bfrb from pseudomonas aeruginosa in complex with a protein-protein interaction inhibitor (analog 12)
Analyse 1.65 a resolution structure of apo bfrb from pseudomonas aeruginosa in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NLJ
- Type
- protein
- Length
- 1,865 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ferroxidase
- EC
- 1.16.3.1
- UniProt
- Q9HY79
- Ligands
- KTV, K
- Pockets
- 20 · best druggability 0.73
Structure
x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E, F, I, J, K | Ferroxidase (EC 1.16.3.1) | protein | 155 | 79% helix, 0% strand | Q9HY79 |
| C, D, G, H, L | Ferroxidase (EC 1.16.3.1) | protein | 156 | 78% helix, 0% strand | Q9HY79 |
Ligands and binding sites
- KTV · 4-{[(3-hydroxyphenyl)methyl]amino}-1H-isoindole-1, 3(2H)-dione · ligand · 3 copies · chains D, B, E, F, K
- K · Potassium ion · metal · 3 copies · chains A, E, J, K, B, C, G, L, D, F, I
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 201 | 0.73 | 0.89 | 32 | empty |
| 2 | 77 | 0.72 | 0.96 | 13 | empty |
| 3 | 192 | 0.72 | 0.88 | 32 | empty |
| 4 | 83 | 0.72 | 0.95 | 12 | empty |
| 5 | 207 | 0.72 | 0.87 | 34 | empty |
Interfaces
27 interfaces between chains.
- B–E · 914 Ų buried · 12 hydrogen bonds · protein-protein
- F–K · 914 Ų buried · 10 hydrogen bonds · protein-protein
- C–I · 913 Ų buried · 12 hydrogen bonds · protein-protein
- H–J · 911 Ų buried · 12 hydrogen bonds · protein-protein
- G–I · 558 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 6NLJ · 1.65 A resolution structure of Apo BfrB from Pseudomonas aeruginosa in complex with a… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9HY79
- Elsewhere: RCSB PDB 6NLJ · PDBe 6NLJ · UniProt Q9HY79
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