Research workbench
3-dimensional structure of native CEL7A from talaromyces emersonii
Analyse 3-dimensional structure of native CEL7A from talaromyces emersonii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q9H
- Type
- protein
- Length
- 430 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellobiohydrolase I catalytic domain
- EC
- 3.2.1.91
- Ligands
- NAG
- Pockets
- 2 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cellobiohydrolase I catalytic domain (EC 3.2.1.91) | protein | 430 | 14% helix, 36% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · 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 | 769 | 0.78 | 0.82 | 70 | empty |
| 2 | 51 | 0.69 | 0.98 | 24 | empty |
Modifications
Observed in the structure: 9 disulfide, 2 glycan, 1 modified (disulfide, N-glycosylation, cyclization).
Compared structures
- 1Q9H · 3-Dimensional structure of native Cel7A from Talaromyces emersonii · 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
- Elsewhere: RCSB PDB 1Q9H · PDBe 1Q9H
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