Research workbench
Structure of the bacterial cellulose synthase subunit Z
Analyse Structure of the bacterial cellulose synthase subunit Z in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3QXF
- Type
- protein
- Length
- 1,348 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase
- EC
- 3.2.1.4
- UniProt
- P37651
- Pockets
- 11 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Endoglucanase (EC 3.2.1.4) | protein | 337 | 48% helix, 14% strand | P37651 |
Pockets
11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 796 | 0.75 | 0.80 | 85 | empty |
| 2 | 250 | 0.72 | 0.87 | 43 | empty |
| 3 | 484 | 0.63 | 0.76 | 52 | empty |
| 4 | 420 | 0.62 | 0.77 | 50 | empty |
| 5 | 227 | 0.57 | 0.78 | 32 | empty |
Interfaces
4 interfaces between chains.
- B–C · 501 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 467 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 409 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 298 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 36 modified (engineered).
Compared structures
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 P37651
- Elsewhere: RCSB PDB 3QXF · PDBe 3QXF · UniProt P37651
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.