Research workbench
Biochemical and structural insights into the catalytic mechanism of thermostable cellobiohydrolase CEL7A from industrially relevant fungus myceliophthora thermophila
Analyse Biochemical and structural insights into the catalytic mechanism of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5W11
- Type
- protein
- Length
- 877 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucanase
- EC
- 3.2.1.176
- UniProt
- G2Q665
- Ligands
- BGC, NAG, MAN, GLC
- Pockets
- 3 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucanase (EC 3.2.1.176) | protein | 437 | 13% helix, 36% strand | G2Q665 |
| B | Glucanase (EC 3.2.1.176) | protein | 440 | 13% helix, 36% strand | G2Q665 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 8 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
- MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A, B
- GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B
- 144 · Tris-hydroxymethyl-methyl-ammonium · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 967 | 0.82 | 0.83 | 86 | GLC, BGC |
| 2 | 912 | 0.81 | 0.83 | 85 | GLC, BGC |
| 3 | 959 | 0.73 | 0.77 | 89 | empty |
Interfaces
1 interface between chains.
- A–B · 300 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 disulfide, 4 glycan, 2 modified (disulfide, N-glycosylation, O-glycosylation, cyclization).
Compared structures
- 5W11 · Biochemical and structural insights into the catalytic mechanism of thermostable… · 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 G2Q665
- Elsewhere: RCSB PDB 5W11 · PDBe 5W11 · UniProt G2Q665
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