Research workbench
Dehydroquinate dehydratase and shikimate dehydrogenase from S. pombe arom
Analyse Dehydroquinate dehydratase and shikimate dehydrogenase from S. pombe arom in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5SWV
- Type
- protein
- Length
- 530 residues
- Chains
- 1
- 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
- Q9P7R0
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | 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 | 530 | 40% helix, 21% strand | Q9P7R0 |
Ligands and binding sites
- PGE · Triethylene glycol · additive · 2 copies · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 914 | 0.75 | 0.78 | 75 | empty |
| 2 | 63 | 0.63 | 0.93 | 20 | PGE |
| 3 | 383 | 0.63 | 0.78 | 39 | empty |
| 4 | 65 | 0.42 | 0.81 | 15 | empty |
| 5 | 104 | 0.36 | 0.74 | 15 | empty |
Compared structures
- 5SWV · Dehydroquinate dehydratase and shikimate dehydrogenase from S. pombe AroM · the same entry in another collection · chain C against C, TM-score 1.00
- Q9P7R0 · AlphaFold monomer V2.0 prediction for pentafunctional arom polypeptide (Q9P7R0) · a predicted model of the same protein · chain C against A, TM-score 0.91
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 Q9P7R0
- Elsewhere: RCSB PDB 5SWV · PDBe 5SWV · UniProt Q9P7R0
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