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Structure of the catalytic core domain of the cellobiohydrolase, CEL6A, from chaetomium thermophilum
Analyse Structure of the catalytic core domain of the cellobiohydrolase, CEL6A, from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A05
- Type
- protein
- Length
- 360 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellobiohydrolase family 6
- EC
- 3.2.1.91
- UniProt
- Q4JQF8
- Ligands
- BGC, NAG, LI
- Pockets
- 1 · best druggability 0.72
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellobiohydrolase family 6 (EC 3.2.1.91) | protein | 360 | 38% helix, 13% strand | Q4JQF8 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 6 copies · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
- LI · Lithium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 414 | 0.72 | 0.83 | 56 | BGC, LI |
Modifications
Observed in the structure: 2 disulfide, 1 glycan (disulfide, N-glycosylation).
Compared structures
- 4A05 · Structure of the catalytic core domain of the cellobiohydrolase, Cel6A, from Chaetomium… · 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 Q4JQF8
- Elsewhere: RCSB PDB 4A05 · PDBe 4A05 · UniProt Q4JQF8
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