Research workbench
GH43 endo-arabinanase from bacillus licheniformis
Analyse GH43 endo-arabinanase from bacillus licheniformis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6B7K
- Type
- protein
- Length
- 1,160 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endo-alpha-(1->5)-L-arabinanase
- EC
- 3.2.1.99
- UniProt
- Q65GB9
- Ligands
- CA
- Pockets
- 12 · best druggability 0.89
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Endo-alpha-(1->5)-L-arabinanase (EC 3.2.1.99) | protein | 290 | 6% helix, 51% strand | Q65GB9 |
Ligands and binding sites
- CA · Calcium ion · metal · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 972 | 0.89 | 0.90 | 84 | CA |
| 2 | 478 | 0.81 | 0.88 | 71 | empty |
| 3 | 349 | 0.79 | 0.89 | 52 | empty |
| 4 | 80 | 0.55 | 0.86 | 21 | empty |
| 5 | 205 | 0.54 | 0.78 | 29 | empty |
Interfaces
5 interfaces between chains.
- B–C · 842 Ų buried · 12 hydrogen bonds · protein-protein
- C–D · 591 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 562 Ų buried · 5 hydrogen bonds · protein-protein
- B–D · 139 Ų buried · 1 hydrogen bond · protein-protein
- A–C · 131 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6B7K · GH43 Endo-Arabinanase from Bacillus licheniformis · 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 Q65GB9
- Elsewhere: RCSB PDB 6B7K · PDBe 6B7K · UniProt Q65GB9
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