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Crystal structure of a putative thua-like protein (BACUNI_01602) from bacteroides uniformis atcc 8492 at 1.50 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
- 4PXY
- Type
- protein
- Length
- 488 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- A7V213
- Ligands
- ZN, CL
- Pockets
- 7 · best druggability 0.53
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Uncharacterized protein | protein | 244 | 30% helix, 26% strand | A7V213 |
Ligands and binding sites
- ZN · Zinc ion · metal · 13 copies · chains A, B
- CL · Chloride ion · ion · 6 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 5 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.53 | 0.83 | 21 | EDO |
| 2 | 190 | 0.50 | 0.77 | 28 | empty |
| 3 | 160 | 0.46 | 0.76 | 26 | empty |
| 4 | 78 | 0.34 | 0.74 | 10 | empty |
| 5 | 61 | 0.33 | 0.76 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 858 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 4PXY · 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 4PXY · PDBe 4PXY · UniProt A7V213
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