MolNFT v1 · #13136 · protein
The crystal structure and catalytic mechanism of cellobiohydrolase cels, the major enzymatic component of the clostridium thermocellum cellulosome
1L2A: “The crystal structure and catalytic mechanism of cellobiohydrolase cels, the major enzymatic component of the…”. X-ray diffraction, 1 ligand (BGC), 20 pockets (best druggability 0.88). MolNFT v1 #13136 on GenesisL1: 3D structure…
- PDB
- 1L2A
- 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 · 48 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 | 945 | 0.88 | 0.89 | 86 | BGC |
| 2 | 1130 | 0.87 | 0.88 | 103 | BGC |
| 3 | 1126 | 0.87 | 0.88 | 104 | BGC |
| 4 | 1085 | 0.87 | 0.88 | 97 | BGC |
| 5 | 1146 | 0.87 | 0.88 | 101 | BGC |
Interfaces
11 interfaces between chains.
- A–D · 930 Ų buried · 12 hydrogen bonds · protein-protein
- C–F · 833 Ų buried · 12 hydrogen bonds · protein-protein
- E–F · 613 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 603 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 498 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1L2A · 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 1L2A · PDBe 1L2A · UniProt P38686
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