Research workbench
Structure of E70A mutant of REX8A from paenibacillus barcinonensis.
Analyse Structure of E70A mutant of REX8A from paenibacillus barcinonensis. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TPP
- Type
- protein
- Length
- 754 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Reducing-end xylose-releasing exo-oligoxylanase REX8A
- EC
- 3.2.1.156
- UniProt
- A0A0S2UQQ5
- Pockets
- 4 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 51% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Reducing-end xylose-releasing exo-oligoxylanase REX8A (EC 3.2.1.156) | protein | 377 | 51% helix, 10% strand | A0A0S2UQQ5 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1154 | 0.83 | 0.84 | 111 | EDO |
| 2 | 67 | 0.76 | 0.99 | 20 | empty |
| 3 | 60 | 0.75 | 1.00 | 19 | empty |
| 4 | 205 | 0.46 | 0.74 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 566 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6TPP · Structure of E70A mutant of Rex8A from Paenibacillus barci nsis. · 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 A0A0S2UQQ5
- Elsewhere: RCSB PDB 6TPP · PDBe 6TPP · UniProt A0A0S2UQQ5
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