MolNFT v1 · #137842 · protein
Biochemical and structural insights into the catalytic mechanism of thermostable cellobiohydrolase CEL7A from industrially relevant fungus myceliophthora thermophila
5W11 · Glucanase: “Biochemical and structural insights into the catalytic mechanism of thermostable cellobiohydrolase CEL7A from…”. X-ray diffraction, 4 ligands (BGC, NAG, MAN), 3 pockets (best druggability 0.82). MolNFT v1 #137842 on…
- 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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