Research workbench
Crystal structure of a taxus phenylalanine aminomutase
Analyse Crystal structure of a taxus phenylalanine aminomutase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NZ4
- Type
- protein
- Length
- 1,310 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phenylalanine ammonia-lyase
- EC
- 4.3.1.24
- UniProt
- Q6GZ04
- Ligands
- TCA
- Pockets
- 13 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phenylalanine ammonia-lyase (EC 4.3.1.24) | protein | 654 | 64% helix, 4% strand | Q6GZ04 |
| B | Phenylalanine ammonia-lyase (EC 4.3.1.24) | protein | 656 | 62% helix, 5% strand | Q6GZ04 |
Ligands and binding sites
- TCA · Phenylethylenecarboxylic acid · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 132 | 0.63 | 0.87 | 18 | empty |
| 2 | 282 | 0.61 | 0.79 | 47 | empty |
| 3 | 187 | 0.54 | 0.79 | 34 | empty |
| 4 | 269 | 0.53 | 0.76 | 31 | empty |
| 5 | 187 | 0.52 | 0.78 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 4037 Ų buried · 65 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (nonstandard).
Compared structures
- 3NZ4 · Crystal Structure of a Taxus Phenylalanine Aminomutase · the same entry in another collection · chain B against B, TM-score 1.00
- Q6GZ04 · AlphaFold monomer V2.0 prediction for phenylalanine aminomutase (L-beta-phenylalanine… · a predicted model of the same protein · chain B 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 Q6GZ04
- Elsewhere: RCSB PDB 3NZ4 · PDBe 3NZ4 · UniProt Q6GZ04
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