Research workbench
Structural investigations into the stereochemistry and activity of a phenylalanine-2,3-aminomutase from taxus chinensis
Analyse Structural investigations into the stereochemistry and activity of a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C5S
- Type
- protein
- Length
- 2,563 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenylalanine ammonia-lyase
- EC
- 4.3.1.24
- UniProt
- Q68G84
- Ligands
- BQ7
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 3 distinct chains · 65% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenylalanine ammonia-lyase (EC 4.3.1.24) | protein | 639 | 65% helix, 5% strand | Q68G84 |
| B, D | Phenylalanine ammonia-lyase (EC 4.3.1.24) | protein | 641 | 65% helix, 5% strand | Q68G84 |
| C | Phenylalanine ammonia-lyase (EC 4.3.1.24) | protein | 642 | 64% helix, 5% strand | Q68G84 |
Ligands and binding sites
- BQ7 · (3S)-3-amino-2,2-difluoro-3-phenylpropanoic acid · ligand · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1069 | 0.81 | 0.82 | 111 | empty |
| 2 | 778 | 0.80 | 0.84 | 89 | empty |
| 3 | 77 | 0.76 | 0.98 | 26 | BQ7 |
| 4 | 76 | 0.76 | 0.99 | 27 | BQ7 |
| 5 | 75 | 0.75 | 0.98 | 27 | BQ7 |
Interfaces
6 interfaces between chains.
- A–B · 4026 Ų buried · 62 hydrogen bonds · protein-protein
- C–D · 4014 Ų buried · 59 hydrogen bonds · protein-protein
- B–D · 3820 Ų buried · 63 hydrogen bonds · protein-protein
- A–C · 3801 Ų buried · 63 hydrogen bonds · protein-protein
- A–D · 1255 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 covalent, 4 modified (covalent ligand, nonstandard).
Compared structures
- Q68G84 · AlphaFold monomer V2.0 prediction for phenylalanine aminomutase (L-beta-phenylalanine… · a predicted model of the same protein · chain A against A, TM-score 1.00
- 4C5S · Structural Investigations into the Stereochemistry and Activity of a… · the same entry in another collection · chain C against C, 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 Q68G84
- Elsewhere: RCSB PDB 4C5S · PDBe 4C5S · UniProt Q68G84
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.