Research workbench
Structure of the thermostable GH51 alpha-L-arabinofuranosidase from thermotoga petrophila rku-1
Analyse Structure of the thermostable GH51 alpha-L-arabinofuranosidase from thermotoga… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3S2C
- Type
- protein
- Length
- 5,794 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-N-arabinofuranosidase
- EC
- 3.2.1.55
- UniProt
- A5IKC8
- Pockets
- 20 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, K, L | Alpha-N-arabinofuranosidase (EC 3.2.1.55) | protein | 483 | 28% helix, 31% strand | A5IKC8 |
| J | Alpha-N-arabinofuranosidase (EC 3.2.1.55) | protein | 481 | 28% helix, 28% strand | A5IKC8 |
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 | 1151 | 0.74 | 0.77 | 112 | empty |
| 2 | 993 | 0.74 | 0.77 | 54 | empty |
| 3 | 1086 | 0.73 | 0.76 | 67 | empty |
| 4 | 930 | 0.72 | 0.77 | 52 | empty |
| 5 | 525 | 0.70 | 0.80 | 72 | empty |
Interfaces
19 interfaces between chains.
- B–C · 756 Ų buried · 8 hydrogen bonds · protein-protein
- I–J · 747 Ų buried · 5 hydrogen bonds · protein-protein
- A–F · 734 Ų buried · 9 hydrogen bonds · protein-protein
- C–E · 730 Ų buried · 8 hydrogen bonds · protein-protein
- J–L · 726 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 3S2C · Structure of the thermostable GH51 alpha-L-arabinofuranosidase from Thermotoga petrophila… · 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 A5IKC8
- Elsewhere: RCSB PDB 3S2C · PDBe 3S2C · UniProt A5IKC8
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