Research workbench
Crystal structure of a DUF861 family protein with a rmlc-like cupin fold (BB1179) from bordetella bronchiseptica RB50 at 1.60 a resolution
Analyse Crystal structure of a DUF861 family protein with a rmlc-like cupin fold… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BCW
- Type
- protein
- Length
- 237 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- Q7WN61
- Pockets
- 2 · best druggability 0.56
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 60% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 118 | 0% helix, 61% strand | Q7WN61 |
| B | Uncharacterized protein | protein | 119 | 0% helix, 60% strand | Q7WN61 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 8 copies · chains A, B
- ACT · Acetate ion · additive · chains A
- PEG · Di(hydroxyethyl)ether · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 214 | 0.56 | 0.79 | 24 | EDO |
| 2 | 200 | 0.54 | 0.78 | 25 | ACT, EDO |
Interfaces
1 interface between chains.
- A–B · 1677 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 3BCW · Crystal structure of a duf861 family protein with a rmlc-like cupin fold (bb1179) from… · 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 Q7WN61
- Elsewhere: RCSB PDB 3BCW · PDBe 3BCW · UniProt Q7WN61
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