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Crystal structure of the N-terminal fic domain of a putative cell filamentation protein (virb-translocated bep effector protein) from bartonella quintana
Analyse Crystal structure of the N-terminal fic domain of a putative cell filamentation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4LU4
- Type
- protein
- Length
- 440 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative cell filamentation protein
- UniProt
- Q6FYV8
- Ligands
- IOD, CL, BR
- Pockets
- 6 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 57% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative cell filamentation protein | protein | 220 | 57% helix, 5% strand | Q6FYV8 |
Ligands and binding sites
- IOD · Iodide ion · ion · 11 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
- BR · Bromide ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 532 | 0.63 | 0.75 | 49 | empty |
| 2 | 326 | 0.57 | 0.76 | 40 | IOD |
| 3 | 320 | 0.56 | 0.76 | 34 | IOD |
| 4 | 131 | 0.43 | 0.76 | 23 | BR |
| 5 | 69 | 0.37 | 0.78 | 14 | IOD |
Interfaces
1 interface between chains.
- A–B · 250 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4LU4 · Crystal Structure of the N-terminal Fic Domain of a Putative Cell Filamentation protein… · the same entry in another collection · chain B against B, 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 Q6FYV8
- Elsewhere: RCSB PDB 4LU4 · PDBe 4LU4 · UniProt Q6FYV8
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