Research workbench
Crystal structure of cellobiohydrolase from melanocarpus albomyces complexed with cellotriose
Analyse Crystal structure of cellobiohydrolase from melanocarpus albomyces complexed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2RFZ
- Type
- protein
- Length
- 1,720 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellulose 1,4-beta-cellobiosidase
- EC
- 3.2.1.91
- UniProt
- Q8J0K6
- Ligands
- BGC, GLC
- Pockets
- 16 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 8% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Cellulose 1,4-beta-cellobiosidase (EC 3.2.1.91) | protein | 430 | 8% helix, 31% strand | Q8J0K6 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 12 copies · chains A, D, B, C
- GLC · alpha-D-glucopyranose · sugar · 6 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 972 | 0.85 | 0.86 | 90 | GLC, BGC |
| 2 | 883 | 0.84 | 0.86 | 91 | GLC, BGC |
| 3 | 715 | 0.83 | 0.87 | 83 | GLC, BGC |
| 4 | 809 | 0.83 | 0.86 | 72 | GLC, BGC |
| 5 | 86 | 0.75 | 0.97 | 25 | empty |
Interfaces
4 interfaces between chains.
- B–C · 877 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 868 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 331 Ų buried · 2 hydrogen bonds · protein-protein
- C–D · 281 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 36 disulfide, 4 modified (disulfide, cyclization).
Compared structures
- 2RFZ · Crystal structure of cellobiohydrolase from Melanocarpus albomyces complexed with… · 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 Q8J0K6
- Elsewhere: RCSB PDB 2RFZ · PDBe 2RFZ · UniProt Q8J0K6
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