Research workbench
Dehydroquinate dehydratase from a. fumigatus arom
Analyse Dehydroquinate dehydratase from a. fumigatus arom in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5SWU
- Type
- protein
- Length
- 502 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pentafunctional arom polypeptide
- EC
- 4.2.3.4, 2.5.1.19, 2.7.1.71, 4.2.1.10, 1.1.1.25
- UniProt
- B0XRM8
- Pockets
- 6 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Pentafunctional arom polypeptide (EC 4.2.3.4, 2.5.1.19, 2.7.1.71, 4.2.1.10, 1.1.1.25) | protein | 251 | 39% helix, 18% strand | B0XRM8 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 659 | 0.73 | 0.79 | 55 | empty |
| 2 | 230 | 0.65 | 0.83 | 47 | empty |
| 3 | 260 | 0.63 | 0.81 | 31 | empty |
| 4 | 125 | 0.42 | 0.76 | 27 | empty |
| 5 | 71 | 0.41 | 0.80 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 881 Ų buried · 12 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 B0XRM8
- Elsewhere: RCSB PDB 5SWU · PDBe 5SWU · UniProt B0XRM8
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