Research workbench
Native structure of trichoderma reesei carbohydrate-active enzymes family AA12
Analyse Native structure of trichoderma reesei carbohydrate-active enzymes family AA12 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6H7T
- Type
- protein
- Length
- 400 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Soluble quino protein glucose dehydrogenase
- UniProt
- A0A024S820
- Ligands
- NAG, BMA, CA
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Soluble quino protein glucose dehydrogenase | protein | 400 | 7% helix, 39% strand | A0A024S820 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 7 copies · chains A
- BMA · beta-D-mannopyranose · sugar
- CA · Calcium ion · metal · chains A
- PGE · Triethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.64 | 0.79 | 45 | empty |
| 2 | 195 | 0.49 | 0.76 | 25 | empty |
| 3 | 88 | 0.37 | 0.75 | 20 | empty |
Modifications
Observed in the structure: 5 glycan, 2 disulfide (N-glycosylation, disulfide).
Compared structures
- 6H7T · Native structure of Trichoderma reesei Carbohydrate-Active Enzymes Family AA12 · 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 A0A024S820
- Elsewhere: RCSB PDB 6H7T · PDBe 6H7T · UniProt A0A024S820
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