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Structure of the endo-1,4-beta-glucanase from bacillus subtilis 168 with MANGANESE(II) ion
Analyse Structure of the endo-1,4-beta-glucanase from bacillus subtilis 168 with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PZT
- Type
- protein
- Length
- 589 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endoglucanase
- EC
- 3.2.1.4
- UniProt
- P10475
- Ligands
- MN, PO4
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endoglucanase (EC 3.2.1.4) | protein | 293 | 40% helix, 19% strand | P10475 |
| B | Endoglucanase (EC 3.2.1.4) | protein | 296 | 40% helix, 19% strand | P10475 |
Ligands and binding sites
- MN · Manganese (II) ion · metal · 2 copies · chains A, B
- PO4 · Phosphate ion · ion · chains B
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 550 | 0.69 | 0.79 | 65 | GOL |
| 2 | 94 | 0.36 | 0.75 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 527 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 3PZT · Structure of the endo-1,4-beta-glucanase from Bacillus subtilis 168 with manganese(II) ion · the same entry in another collection · chain A against A, TM-score 1.00
- P10475 · AlphaFold monomer V2.0 prediction for endoglucanase (P10475) · a predicted model of the same protein · chain B 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 P10475
- Elsewhere: RCSB PDB 3PZT · PDBe 3PZT · UniProt P10475
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