MolNFT v1 · #120663 · protein
Crystal structure of elongation factor 2 GDP-form
5H7K: “Crystal structure of elongation factor 2 GDP-form”. X-ray diffraction, 1 ligand (GDP), 2 pockets (best druggability 0.60). MolNFT v1 #120663 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5H7K
- Type
- protein
- Length
- 367 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor 2
- UniProt
- O59521
- Ligands
- GDP
- Pockets
- 2 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor 2 | protein | 367 | 36% helix, 26% strand | O59521 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.60 | 0.86 | 34 | empty |
| 2 | 54 | 0.35 | 0.79 | 15 | empty |
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 O59521
- Elsewhere: RCSB PDB 5H7K · PDBe 5H7K · UniProt O59521
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