Research workbench
Complex structure of lf-transferase and leucine
Analyse Complex structure of lf-transferase and leucine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Z3P
- 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
- LEU
- Pockets
- 3 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | LEUCYL/PHENYLALANYL-tRNA-protein transferase (EC 2.3.2.6) | protein | 232 | 34% helix, 27% strand | P0A8P1 |
| B | LEUCYL/PHENYLALANYL-tRNA-protein transferase (EC 2.3.2.6) | protein | 231 | 34% helix, 26% strand | P0A8P1 |
Ligands and binding sites
- LEU · Leucine · 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 | 535 | 0.81 | 0.87 | 56 | empty |
| 2 | 301 | 0.67 | 0.82 | 35 | LEU |
| 3 | 347 | 0.67 | 0.80 | 36 | LEU |
Interfaces
1 interface between chains.
- A–B · 910 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
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 2Z3P · PDBe 2Z3P · UniProt P0A8P1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.