Research workbench
Crystal structure of L-arabinose isomerase from E.COLI
Analyse Crystal structure of L-arabinose isomerase from E.COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AJT
- Type
- protein
- Length
- 1,494 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-arabinose isomerase
- EC
- 5.3.1.4
- UniProt
- P08202
- Pockets
- 15 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | L-arabinose isomerase (EC 5.3.1.4) | protein | 498 | 41% helix, 22% strand | P08202 |
Pockets
15 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 681 | 0.81 | 0.85 | 70 | empty |
| 2 | 690 | 0.80 | 0.85 | 66 | empty |
| 3 | 583 | 0.79 | 0.85 | 59 | empty |
| 4 | 268 | 0.76 | 0.88 | 36 | empty |
| 5 | 84 | 0.76 | 0.98 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–B · 2324 Ų buried · 29 hydrogen bonds · protein-protein
- B–C · 2311 Ų buried · 32 hydrogen bonds · protein-protein
- A–C · 2047 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
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 P08202
- Elsewhere: RCSB PDB 2AJT · PDBe 2AJT · UniProt P08202
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