Research workbench
Structure of a GH5 family lichenase from caldicellulosiruptor sp. F32
Analyse Structure of a GH5 family lichenase from caldicellulosiruptor sp. F32 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4X0V
- Type
- protein
- Length
- 2,995 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-1,3-1,4-glucanase
- EC
- 3.2.1.-
- UniProt
- R9RX81
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D | Beta-1,3-1,4-glucanase (EC 3.2.1.-) | protein | 375 | 39% helix, 13% strand | R9RX81 |
| C | Beta-1,3-1,4-glucanase (EC 3.2.1.-) | protein | 376 | 38% helix, 13% strand | R9RX81 |
| E, H | Beta-1,3-1,4-glucanase (EC 3.2.1.-) | protein | 373 | 38% helix, 13% strand | R9RX81 |
| F, G | Beta-1,3-1,4-glucanase (EC 3.2.1.-) | protein | 374 | 40% helix, 13% strand | R9RX81 |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 953 | 0.80 | 0.82 | 96 | empty |
| 2 | 740 | 0.80 | 0.83 | 79 | empty |
| 3 | 992 | 0.79 | 0.81 | 85 | empty |
| 4 | 881 | 0.79 | 0.81 | 82 | empty |
| 5 | 728 | 0.73 | 0.79 | 71 | empty |
Interfaces
12 interfaces between chains.
- F–H · 905 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 892 Ų buried · 10 hydrogen bonds · protein-protein
- D–E · 865 Ų buried · 12 hydrogen bonds · protein-protein
- D–G · 858 Ų buried · 12 hydrogen bonds · protein-protein
- B–G · 846 Ų buried · 11 hydrogen bonds · protein-protein
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 R9RX81
- Elsewhere: RCSB PDB 4X0V · PDBe 4X0V · UniProt R9RX81
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