MolNFT v1 · #88286 · protein
Structural investigations into the stereochemistry and activity of a phenylalanine-2,3-aminomutase from taxus chinensis
4CQ5 · Phenylalanine aminomutase: “Structural investigations into the stereochemistry and activity of a phenylalanine-2,3-aminomutase from taxus…”. X-ray diffraction, 1 ligand (TCA), 20 pockets (best druggability 0.81). MolNFT v1 #88286 on…
- PDB
- 4CQ5
- Type
- protein
- Length
- 2,560 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenylalanine aminomutase
- UniProt
- Q68G84
- Ligands
- TCA
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 4 distinct chains · 64% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenylalanine aminomutase | protein | 639 | 65% helix, 4% strand | Q68G84 |
| B | Phenylalanine aminomutase | protein | 638 | 64% helix, 5% strand | Q68G84 |
| C | Phenylalanine aminomutase | protein | 641 | 64% helix, 5% strand | Q68G84 |
| D | Phenylalanine aminomutase | protein | 642 | 65% helix, 5% strand | Q68G84 |
Ligands and binding sites
- TCA · Phenylethylenecarboxylic acid · ligand · 8 copies · chains A, B, C, D
- GOL · Glycerol · additive · chains B, D
- EDO · 1,2-ethanediol · additive · chains B, 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, 16 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 977 | 0.81 | 0.82 | 93 | empty |
| 2 | 741 | 0.79 | 0.83 | 89 | empty |
| 3 | 82 | 0.77 | 0.99 | 26 | TCA |
| 4 | 84 | 0.77 | 0.98 | 26 | TCA |
| 5 | 75 | 0.76 | 0.99 | 26 | TCA |
Interfaces
6 interfaces between chains.
- C–D · 4030 Ų buried · 58 hydrogen bonds · protein-protein
- A–B · 4027 Ų buried · 63 hydrogen bonds · protein-protein
- B–D · 3916 Ų buried · 60 hydrogen bonds · protein-protein
- A–C · 3890 Ų buried · 59 hydrogen bonds · protein-protein
- B–C · 1244 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (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
- 4CQ5 · Structural Investigations into the Stereochemistry and Activity of a… · the same entry in another collection · chain D against D, 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 4CQ5 · PDBe 4CQ5 · UniProt Q68G84
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