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Crystal structure (P21 form) of a GH128 (subgroup IV) endo-beta-1,3- glucanase from lentinula edodes (LEGH128_IV) in complex with laminaritriose
Analyse Crystal structure (P21 form) of a GH128 (subgroup IV) endo-beta-1,3- glucanase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UB5
- Type
- protein
- Length
- 251 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-beta-1,3-glucanase
- UniProt
- G9M5R4
- Ligands
- BGC, CL
- Pockets
- 1 · best druggability 0.40
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endo-beta-1,3-glucanase | protein | 251 | 34% helix, 20% strand | G9M5R4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 144 | 0.40 | 0.74 | 25 | BGC |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6UB5 · Crystal structure (P21 form) of a GH128 (subgroup IV) endo-beta-1,3-glucanase from… · 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 G9M5R4
- Elsewhere: RCSB PDB 6UB5 · PDBe 6UB5 · UniProt G9M5R4
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