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The crystal structure of prephenate dehydratase in complex with L-phe from arthrobacter aurescens to 2.0A
Analyse The crystal structure of prephenate dehydratase in complex with L-phe from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3MWB
- Type
- protein
- Length
- 609 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prephenate dehydratase
- EC
- 4.2.1.51
- UniProt
- A1R118
- Ligands
- PHE, MG
- Pockets
- 5 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 31% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Prephenate dehydratase (EC 4.2.1.51) | protein | 306 | 30% helix, 28% strand | A1R118 |
| B | Prephenate dehydratase (EC 4.2.1.51) | protein | 303 | 32% helix, 29% strand | A1R118 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1081 | 0.82 | 0.83 | 122 | empty |
| 2 | 60 | 0.71 | 0.97 | 20 | PHE |
| 3 | 54 | 0.70 | 0.97 | 20 | PHE |
| 4 | 258 | 0.50 | 0.74 | 28 | empty |
| 5 | 137 | 0.49 | 0.79 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1479 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 modified (engineered).
Compared structures
- 3MWB · The Crystal Structure of Prephenate dehydratase in complex with L-Phe from Arthrobacter… · 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 A1R118
- Elsewhere: RCSB PDB 3MWB · PDBe 3MWB · UniProt A1R118
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