Research workbench
Crystal structure of a branched chain amino acid ABC transporter periplasmic ligand-binding protein (BXE_C0949) from burkholderia xenovorans LB400 at 1.88 a resolution
Analyse Crystal structure of a branched chain amino acid ABC transporter periplasmic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3N0W
- Type
- protein
- Length
- 748 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC branched chain amino acid family transporter, periplasmic ligand binding protein
- UniProt
- Q13GG5
- Ligands
- NI
- Pockets
- 5 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ABC branched chain amino acid family transporter, periplasmic ligand binding protein | protein | 374 | 44% helix, 20% strand | Q13GG5 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 867 | 0.71 | 0.76 | 62 | empty |
| 2 | 382 | 0.64 | 0.79 | 52 | empty |
| 3 | 389 | 0.59 | 0.76 | 39 | empty |
| 4 | 129 | 0.59 | 0.84 | 27 | empty |
| 5 | 132 | 0.58 | 0.84 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 248 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified, 2 disulfide (engineered, disulfide).
Compared structures
- 3N0W · Crystal structure of a branched chain amino acid ABC transporter periplasmic… · 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 Q13GG5
- Elsewhere: RCSB PDB 3N0W · PDBe 3N0W · UniProt Q13GG5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.