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2.22 ångström crystal structure of N-terminal fragment (residues 1- 419) of elongation factor G from legionella pneumophila.
Analyse 2.22 ångström crystal structure of N-terminal fragment (residues 1- 419) of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TY0
- Type
- protein
- Length
- 378 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor G
- UniProt
- Q5ZYP6
- Ligands
- BGC, NA
- Pockets
- 7 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 29% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor G | protein | 378 | 29% helix, 31% strand | Q5ZYP6 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 50 | 0.68 | 0.97 | 17 | empty |
| 2 | 127 | 0.54 | 0.82 | 21 | NA |
| 3 | 75 | 0.40 | 0.79 | 17 | empty |
| 4 | 90 | 0.39 | 0.77 | 23 | empty |
| 5 | 65 | 0.32 | 0.75 | 14 | empty |
Compared structures
- 5TY0 · 2.22 Angstrom Crystal Structure of N-terminal Fragment (residues 1-419) of Elongation… · the same entry in another collection · chain A against A, TM-score 1.00
- Q5ZYP6 · AlphaFold monomer V2.0 prediction for elongation factor G (Q5ZYP6) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q5ZYP6
- Elsewhere: RCSB PDB 5TY0 · PDBe 5TY0 · UniProt Q5ZYP6
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