MolNFT v1 · #138075 · protein
Crystal structure of reconstructed bacterial elongation factor node 168
5W7Q · Consensus elongation factor: “Crystal structure of reconstructed bacterial elongation factor node 168”. X-ray diffraction, 2 ligands (GDP, MG), 2 pockets (best druggability 0.46). MolNFT v1 #138075 on GenesisL1: 3D structure…
- PDB
- 5W7Q
- Type
- protein
- Length
- 371 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Consensus elongation factor
- Ligands
- GDP, MG
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 25% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Consensus elongation factor | protein | 371 | 25% helix, 36% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 258 | 0.46 | 0.72 | 35 | empty |
| 2 | 50 | 0.30 | 0.76 | 19 | MG, GDP |
Compared structures
- 5W7Q · Crystal Structure of Reconstructed Bacterial Elongation Factor Node 168 · the same entry in another collection · 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
- Elsewhere: RCSB PDB 5W7Q · PDBe 5W7Q
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