Research workbench
Crystal structure of a DUF4450 family protein (BT_4147) from bacteroides thetaiotaomicron vpi-5482 at 2.90 a resolution
Analyse Crystal structure of a DUF4450 family protein (BT_4147) from bacteroides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4E0E
- Type
- protein
- Length
- 676 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative uncharacterized protein
- UniProt
- Q8A074
- Pockets
- 9 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Putative uncharacterized protein | protein | 169 | 9% helix, 46% strand | Q8A074 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 922 | 0.71 | 0.76 | 84 | empty |
| 2 | 652 | 0.67 | 0.76 | 54 | empty |
| 3 | 424 | 0.64 | 0.78 | 46 | empty |
| 4 | 378 | 0.63 | 0.78 | 45 | empty |
| 5 | 57 | 0.47 | 0.85 | 16 | empty |
Interfaces
5 interfaces between chains.
- C–D · 2086 Ų buried · 24 hydrogen bonds · protein-protein
- A–B · 2009 Ų buried · 15 hydrogen bonds · protein-protein
- B–C · 373 Ų buried · 10 hydrogen bonds · protein-protein
- B–D · 185 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 184 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 4E0E · Crystal structure of a DUF4450 family protein (BT_4147) from Bacteroides thetaiotaomicron… · 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 Q8A074
- Elsewhere: RCSB PDB 4E0E · PDBe 4E0E · UniProt Q8A074
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