Research workbench
Low-resolution structure of cyclohexadienyl dehydratase from pseudomonas aeruginosa in space group P4322.
Analyse Low-resolution structure of cyclohexadienyl dehydratase from pseudomonas… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BQE
- Type
- protein
- Length
- 720 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arogenate dehydratase
- UniProt
- A0A232A1P4
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 41% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Arogenate dehydratase | protein | 240 | 41% helix, 23% strand | A0A232A1P4 |
Ligands and binding sites
- ACT · Acetate ion · additive · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 672 | 0.73 | 0.79 | 45 | empty |
| 2 | 296 | 0.56 | 0.76 | 26 | empty |
| 3 | 257 | 0.55 | 0.76 | 26 | empty |
| 4 | 246 | 0.54 | 0.76 | 27 | empty |
| 5 | 59 | 0.27 | 0.73 | 17 | empty |
Interfaces
3 interfaces between chains.
- B–C · 723 Ų buried · 12 hydrogen bonds · protein-protein
- A–B · 717 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 709 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 6BQE · Low-resolution structure of cyclohexadienyl dehydratase from Pseudomonas aeruginosa in… · 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 A0A232A1P4
- Elsewhere: RCSB PDB 6BQE · PDBe 6BQE · UniProt A0A232A1P4
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