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The crystal structure and catalytic mechanism of cellobiohydrolase cels, the major enzymatic component of the clostridium thermocellum cellulosome
Analyse The crystal structure and catalytic mechanism of cellobiohydrolase cels, the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1L1Y
- Type
- protein
- Length
- 3,852 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cellobiohydrolase
- EC
- 3.2.1.4
- UniProt
- P38686
- Ligands
- BGC
- Pockets
- 20 · best druggability 0.88
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Cellobiohydrolase (EC 3.2.1.4) | protein | 642 | 40% helix, 16% strand | P38686 |
Ligands and binding sites
- BGC · beta-D-glucopyranose · sugar · 12 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 996 | 0.88 | 0.89 | 105 | BGC |
| 2 | 1070 | 0.87 | 0.88 | 109 | BGC |
| 3 | 1138 | 0.86 | 0.87 | 104 | BGC |
| 4 | 1191 | 0.85 | 0.86 | 125 | BGC |
| 5 | 1176 | 0.85 | 0.86 | 109 | BGC |
Interfaces
11 interfaces between chains.
- A–D · 960 Ų buried · 14 hydrogen bonds · protein-protein
- C–F · 843 Ų buried · 12 hydrogen bonds · protein-protein
- E–F · 625 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 615 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 517 Ų buried · 7 hydrogen bonds · protein-protein
Compared structures
- 1L1Y · The Crystal Structure and Catalytic Mechanism of Cellobiohydrolase CelS, the Major… · 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 P38686
- Elsewhere: RCSB PDB 1L1Y · PDBe 1L1Y · UniProt P38686
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