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The structure of abnb-E201A, an intracellular 1,5-alpha-L-arabinanase from geobacillus stearothermophilus, in complex with arabinopentaose
Analyse The structure of abnb-E201A, an intracellular 1,5-alpha-L-arabinanase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F1G
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Intracellular endo-alpha-(1->5)-L-arabinanase
- EC
- 3.2.1.99
- UniProt
- B3EYM8
- Ligands
- AHR, CA, SO4
- Pockets
- 1 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Intracellular endo-alpha-(1->5)-L-arabinanase (EC 3.2.1.99) | protein | 315 | 4% helix, 48% strand | B3EYM8 |
Ligands and binding sites
- AHR · alpha-L-arabinofuranose · sugar · 5 copies · chains A
- CA · Calcium ion · metal · chains A
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 205 | 0.62 | 0.82 | 30 | AHR |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6F1G · The structure of AbnB-E201A, an intracellular 1,5-alpha-L-arabinanase from Geobacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- B3EYM8 · AlphaFold monomer V2.0 prediction for intracellular endo- alpha-(1->5)-L-arabinanase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 B3EYM8
- Elsewhere: RCSB PDB 6F1G · PDBe 6F1G · UniProt B3EYM8
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