Research workbench
Crystal structure of a putative thua-like protein (BACUNI_01602) from bacteroides uniformis atcc 8492 at 2.30 a resolution
Analyse Crystal structure of a putative thua-like protein (BACUNI_01602) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4JQS
- Type
- protein
- Length
- 735 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hypothetical protein
- UniProt
- A7V213
- Pockets
- 5 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Hypothetical protein | protein | 245 | 29% helix, 27% strand | A7V213 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · 2 copies · chains A, B, C
- P6G · Hexaethylene glycol · additive · chains B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 345 | 0.70 | 0.83 | 54 | empty |
| 2 | 159 | 0.64 | 0.86 | 30 | empty |
| 3 | 187 | 0.63 | 0.84 | 23 | empty |
| 4 | 57 | 0.43 | 0.83 | 16 | empty |
| 5 | 83 | 0.32 | 0.74 | 22 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1271 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 1270 Ų buried · 20 hydrogen bonds · protein-protein
- A–B · 1255 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 modified (engineered).
Compared structures
- 4JQS · Crystal structure of a Putative thua-like protein (BACUNI_01602) 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 A7V213
- Elsewhere: RCSB PDB 4JQS · PDBe 4JQS · UniProt A7V213
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