Research workbench
Pantoea agglomerans phenylalanine aminomutase
Analyse Pantoea agglomerans phenylalanine aminomutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UNV
- Type
- protein
- Length
- 1,028 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Admh
- UniProt
- Q84FL5
- Ligands
- SFE, PHE, PO4
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Admh | protein | 514 | 56% helix, 7% strand | Q84FL5 |
Ligands and binding sites
- SFE · (3S)-3-amino-3-phenylpropanoic acid · ligand · 2 copies · chains A, B
- PHE · Phenylalanine · ligand · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 8 copies · chains A, B
- GOL · Glycerol · additive · 3 copies · chains A, B
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 | 658 | 0.75 | 0.81 | 55 | EDO |
| 2 | 93 | 0.55 | 0.84 | 25 | SFE |
| 3 | 73 | 0.54 | 0.86 | 23 | SFE, PHE |
| 4 | 68 | 0.37 | 0.78 | 18 | GOL |
| 5 | 54 | 0.34 | 0.78 | 17 | EDO |
Interfaces
1 interface between chains.
- A–B · 3398 Ų buried · 41 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent, 2 modified (covalent ligand, nonstandard).
Compared structures
- 3UNV · Pantoea agglomerans Phenylalanine Aminomutase · 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 Q84FL5
- Elsewhere: RCSB PDB 3UNV · PDBe 3UNV · UniProt Q84FL5
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