Research workbench
Crystal structure of BPSL1038 from Burkholderia pseudomallei
Analyse Crystal structure of BPSL1038 from Burkholderia pseudomallei in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VXR
- Type
- protein
- Length
- 187 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.55
- Source
- Burkholderia pseudomallei K96243
- Molecule
- BPSL1038
- UniProt
- Q63W52
- Ligands
- NA
Structure
x-ray diffraction · resolution 1.55 · 2 distinct chains · 42% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | BPSL1038 | protein | 101 | 40% helix, 32% strand | Q63W52 |
| B | BPSL1038 | protein | 86 | 45% helix, 35% strand | Q63W52 |
Ligands and binding sites
- NA · Sodium ion · metal · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 1558 Ų buried · 36 hydrogen bonds · protein-protein
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 Q63W52
- Elsewhere: RCSB PDB 7VXR · PDBe 7VXR · UniProt Q63W52
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