Research workbench
Complex structure of lf-transferase and phenylalanine
Analyse Complex structure of lf-transferase and phenylalanine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z3O
- Type
- protein
- Length
- 463 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- LEUCYL/PHENYLALANYL-tRNA-protein transferase
- EC
- 2.3.2.6
- UniProt
- P0A8P1
- Ligands
- PHE
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | LEUCYL/PHENYLALANYL-tRNA-protein transferase (EC 2.3.2.6) | protein | 232 | 33% helix, 27% strand | P0A8P1 |
| B | LEUCYL/PHENYLALANYL-tRNA-protein transferase (EC 2.3.2.6) | protein | 231 | 32% helix, 26% strand | P0A8P1 |
Ligands and binding sites
- PHE · Phenylalanine · ligand · 2 copies · chains A, B
- TAR · D(-)-tartaric acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 519 | 0.80 | 0.86 | 52 | empty |
| 2 | 333 | 0.68 | 0.82 | 36 | PHE |
| 3 | 267 | 0.65 | 0.82 | 40 | PHE |
Interfaces
1 interface between chains.
- A–B · 920 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 2Z3O · complex structure of LF-transferase and phenylalanine · the same entry in another collection · chain A against A, TM-score 1.00
- P0A8P1 · AlphaFold monomer V2.0 prediction for LEUCYL/PHENYLALANYL-tRNA-- protein transferase… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P0A8P1
- Elsewhere: RCSB PDB 2Z3O · PDBe 2Z3O · UniProt P0A8P1
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