Research workbench
Crystal structure of ABC transporter solute binding protein BB0719 from bordetella bronchiseptica RB50, target efi-510049
Analyse Crystal structure of ABC transporter solute binding protein BB0719 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4N4U
- Type
- protein
- Length
- 606 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative ABC transporter periplasmic solute-binding protein
- UniProt
- Q7WPG5
- Pockets
- 6 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 54% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative ABC transporter periplasmic solute-binding protein | protein | 304 | 54% helix, 21% strand | Q7WPG5 |
| B | Putative ABC transporter periplasmic solute-binding protein | protein | 302 | 53% helix, 19% strand | Q7WPG5 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 449 | 0.63 | 0.76 | 49 | empty |
| 2 | 509 | 0.61 | 0.75 | 54 | empty |
| 3 | 91 | 0.38 | 0.76 | 20 | empty |
| 4 | 78 | 0.31 | 0.73 | 19 | empty |
| 5 | 67 | 0.29 | 0.73 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 621 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 4N4U · Crystal structure of ABC transporter solute binding protein BB0719 from Bordetella… · 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 Q7WPG5
- Elsewhere: RCSB PDB 4N4U · PDBe 4N4U · UniProt Q7WPG5
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