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The three-dimensional structures of two plant beta-glucan endohydrolases with distinct substrate specificities
Analyse The three-dimensional structures of two plant beta-glucan endohydrolases with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1GHR
- Type
- protein
- Length
- 306 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 1,3-1,4-beta-glucanase
- EC
- 3.2.1.73
- UniProt
- P12257
- Pockets
- 2 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 1,3-1,4-beta-glucanase (EC 3.2.1.73) | protein | 306 | 40% helix, 19% strand | P12257 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 87 | 0.35 | 0.75 | 22 | empty |
| 2 | 72 | 0.33 | 0.75 | 22 | empty |
Compared structures
- 1GHR · The three-dimensional structures of two plant beta-glucan endohydrolases with distinct… · the same entry in another collection · chain A against A, TM-score 1.00
- P12257 · AlphaFold monomer V2.0 prediction for lichenase-2 (P12257) · a predicted model of the same protein · 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 P12257
- Elsewhere: RCSB PDB 1GHR · PDBe 1GHR · UniProt P12257
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