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Crystal structure of a NTF2-like protein (BXE_B1094) from burkholderia xenovorans LB400 at 1.59 a resolution
Analyse Crystal structure of a NTF2-like protein (BXE_B1094) from burkholderia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FGY
- Type
- protein
- Length
- 266 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized NTF2-like protein
- UniProt
- Q13M28
- Ligands
- UNL
- Pockets
- 3 · best druggability 0.70
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized NTF2-like protein | protein | 135 | 33% helix, 41% strand | Q13M28 |
| B | Uncharacterized NTF2-like protein | protein | 131 | 34% helix, 43% strand | Q13M28 |
Ligands and binding sites
- UNL · Unknown ligand · ligand · 2 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 304 | 0.70 | 0.83 | 35 | UNL, PEG |
| 2 | 264 | 0.69 | 0.83 | 26 | UNL, PEG |
| 3 | 57 | 0.26 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1026 Ų buried · 24 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 modified (engineered).
Compared structures
- 3FGY · Crystal structure of a NTF2-like protein (BXE_B1094) from burkholderia xenovorans LB400… · 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 Q13M28
- Elsewhere: RCSB PDB 3FGY · PDBe 3FGY · UniProt Q13M28
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