Research workbench
Crystal structure of an ABC transporter (BDI_1369) from parabacteroides distasonis at 1.75 a resolution
Analyse Crystal structure of an ABC transporter (BDI_1369) from parabacteroides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HN0
- Type
- protein
- Length
- 560 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitrate transport protein
- UniProt
- A6LBR3
- Ligands
- PO4
- Pockets
- 6 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nitrate transport protein | protein | 280 | 43% helix, 20% strand | A6LBR3 |
| B | Nitrate transport protein | protein | 280 | 42% helix, 21% strand | A6LBR3 |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 641 | 0.78 | 0.83 | 49 | EDO |
| 2 | 612 | 0.75 | 0.82 | 59 | EDO |
| 3 | 386 | 0.71 | 0.82 | 33 | empty |
| 4 | 240 | 0.54 | 0.77 | 37 | empty |
| 5 | 81 | 0.43 | 0.80 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 774 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 3HN0 · Crystal structure of an ABC transporter (BDI_1369) from parabacteroides distasonis at… · 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 A6LBR3
- Elsewhere: RCSB PDB 3HN0 · PDBe 3HN0 · UniProt A6LBR3
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