Research workbench
Crystal structure of the bacterial cellulose synthase subunit G (bcsg) from escherichia COLI, catalytic domain
Analyse Crystal structure of the bacterial cellulose synthase subunit G (bcsg) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PD0
- Type
- protein
- Length
- 732 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellulose biosynthesis protein bcsg
- UniProt
- P37659
- Ligands
- MG, ZN
- Pockets
- 9 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cellulose biosynthesis protein bcsg | protein | 366 | 32% helix, 20% strand | P37659 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1188 | 0.81 | 0.82 | 152 | empty |
| 2 | 86 | 0.52 | 0.84 | 26 | empty |
| 3 | 115 | 0.43 | 0.77 | 19 | empty |
| 4 | 64 | 0.38 | 0.79 | 18 | empty |
| 5 | 84 | 0.37 | 0.76 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 1045 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6PD0 · Crystal structure of the bacterial cellulose synthase subunit G (BcsG) from Escherichia… · the same entry in another collection · chain A against A, TM-score 1.00
- P37659 · AlphaFold monomer V2.0 prediction for cellulose biosynthesis protein bcsg (P37659) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P37659
- Elsewhere: RCSB PDB 6PD0 · PDBe 6PD0 · UniProt P37659
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