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Crystal structure of CCCEL6C, a glycoside hydrolase family 6 enzyme, from coprinopsis cinerea
Analyse Crystal structure of CCCEL6C, a glycoside hydrolase family 6 enzyme, from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A64
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellobiohydrolase
- EC
- 3.2.1.91
- UniProt
- B7X9Z2
- Ligands
- MG
- Pockets
- 2 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellobiohydrolase (EC 3.2.1.91) | protein | 371 | 41% helix, 11% strand | B7X9Z2 |
Ligands and binding sites
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 751 | 0.73 | 0.79 | 69 | empty |
| 2 | 64 | 0.33 | 0.76 | 13 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 3A64 · Crystal structure of CcCel6C, a glycoside hydrolase family 6 enzyme, from Coprinopsis… · 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 B7X9Z2
- Elsewhere: RCSB PDB 3A64 · PDBe 3A64 · UniProt B7X9Z2
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