Research workbench
Crystal structure of tyrosine aminotransferase tripple mutant (P181Q, R183G,A321K) from escherichia COLI at 2.35 a resolution
Analyse Crystal structure of tyrosine aminotransferase tripple mutant (P181Q… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3FSL
- Type
- protein
- Length
- 2,382 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aromatic-amino-acid aminotransferase
- EC
- 2.6.1.57
- UniProt
- P04693
- Ligands
- PLR
- Pockets
- 20 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Aromatic-amino-acid aminotransferase (EC 2.6.1.57) | protein | 397 | 46% helix, 13% strand | P04693 |
Ligands and binding sites
- PLR · (5-hydroxy-4,6-dimethylpyridin-3-yl)methyl dihydrogen phosphate · ligand · 6 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.80 | 0.93 | 36 | PLR |
| 2 | 260 | 0.79 | 0.92 | 41 | PLR |
| 3 | 285 | 0.77 | 0.89 | 56 | empty |
| 4 | 537 | 0.75 | 0.83 | 66 | PLR |
| 5 | 531 | 0.75 | 0.82 | 71 | PLR |
Interfaces
9 interfaces between chains.
- E–F · 3036 Ų buried · 45 hydrogen bonds · protein-protein
- C–D · 3036 Ų buried · 43 hydrogen bonds · protein-protein
- A–B · 2984 Ų buried · 43 hydrogen bonds · protein-protein
- B–C · 423 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 335 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 covalent (covalent ligand).
Compared structures
- 3FSL · Crystal structure of tyrosine aminotransferase tripple mutant (P181Q,R183G,A321K) from… · the same entry in another collection · chain C against C, TM-score 1.00
- P04693 · AlphaFold monomer V2.0 prediction for aromatic-amino-acid aminotransferase (P04693) · a predicted model of the same protein · 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 P04693
- Elsewhere: RCSB PDB 3FSL · PDBe 3FSL · UniProt P04693
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