Research workbench
E COLI bfr variant Y149F
Analyse E COLI bfr variant Y149F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XKT
- Type
- protein
- Length
- 1,884 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bacterioferritin
- EC
- 1.16.3.1
- UniProt
- E2QFJ1
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Bacterioferritin (EC 1.16.3.1) | protein | 157 | 78% helix, 0% strand | E2QFJ1 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 13 copies · chains B, D, F, C, K, E, G, H, J, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.74 | 0.88 | 32 | empty |
| 2 | 216 | 0.72 | 0.87 | 31 | empty |
| 3 | 203 | 0.71 | 0.87 | 30 | empty |
| 4 | 205 | 0.70 | 0.87 | 31 | empty |
| 5 | 209 | 0.70 | 0.86 | 33 | empty |
Interfaces
24 interfaces between chains.
- E–F · 961 Ų buried · 13 hydrogen bonds · protein-protein
- I–J · 952 Ų buried · 12 hydrogen bonds · protein-protein
- K–L · 945 Ų buried · 12 hydrogen bonds · protein-protein
- G–H · 945 Ų buried · 13 hydrogen bonds · protein-protein
- A–B · 938 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4XKT · E coli BFR variant Y149F · 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 E2QFJ1
- Elsewhere: RCSB PDB 4XKT · PDBe 4XKT · UniProt E2QFJ1
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