Research workbench
CEL6A D175A mutant
Analyse CEL6A D175A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HGW
- Type
- protein
- Length
- 726 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellobiohydrolase CEL6A (formerly called cbh II)
- EC
- 3.2.1.91
- UniProt
- P07987
- Ligands
- MAN, NAG, CO
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Cellobiohydrolase CEL6A (formerly called cbh II) (EC 3.2.1.91) | protein | 363 | 38% helix, 12% strand | P07987 |
Ligands and binding sites
- MAN · alpha-D-mannopyranose · sugar · 14 copies · chains A, B
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B
- CO · Cobalt (II) 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 457 | 0.75 | 0.84 | 51 | empty |
| 2 | 480 | 0.75 | 0.83 | 57 | empty |
Modifications
Observed in the structure: 18 glycan, 4 disulfide (O-glycosylation, disulfide, N-glycosylation).
Compared structures
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 P07987
- Elsewhere: RCSB PDB 1HGW · PDBe 1HGW · UniProt P07987
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