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Crystal structure of an uncharacterized DUF3829-like protein (BT_1908) from bacteroides thetaiotaomicron vpi-5482 at 2.10 a resolution
Analyse Crystal structure of an uncharacterized DUF3829-like protein (BT_1908) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RH3
- Type
- protein
- Length
- 476 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized DUF3829-like protein
- UniProt
- Q8A6H6
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 79% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized DUF3829-like protein | protein | 239 | 79% helix, 0% strand | Q8A6H6 |
| B | Uncharacterized DUF3829-like protein | protein | 237 | 79% helix, 0% strand | Q8A6H6 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1014 | 0.75 | 0.78 | 83 | PEG |
| 2 | 274 | 0.68 | 0.83 | 27 | empty |
| 3 | 178 | 0.62 | 0.84 | 31 | empty |
| 4 | 187 | 0.60 | 0.82 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 213 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 modified (engineered).
Compared structures
- 3RH3 · Crystal structure of an Uncharacterized DUF3829-like protein (BT_1908) from BACTEROIDES… · 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 Q8A6H6
- Elsewhere: RCSB PDB 3RH3 · PDBe 3RH3 · UniProt Q8A6H6
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