MolNFT v1 · #38889 · protein
Trypsin-modified elongation factor tu in complex with tetracycline
2HCJ · Protein chain elongation factor ef-tu: “Trypsin-modified elongation factor tu in complex with tetracycline”. X-ray diffraction, 6 ligands (GDP, TAC, GLV), 1 pocket (best druggability 0.39). MolNFT v1 #38889 on GenesisL1: 3D…
- PDB
- 2HCJ
- Type
- protein
- Length
- 368 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein chain elongation factor ef-tu
- UniProt
- P0A6N1
- Ligands
- GDP, TAC, GLV, NA, MG, SO4
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein chain elongation factor ef-tu | protein | 33 | 48% helix, 21% strand | P0A6N1 |
| B | Protein chain elongation factor ef-tu | protein | 335 | 22% helix, 40% strand | P0A6N1 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A, B
- TAC · Tetracycline · ligand · chains A, B
- GLV · Glyoxylic acid · ligand · chains B
- NA · Sodium ion · metal · 3 copies · chains B, A
- MG · Magnesium ion · metal · chains A, B
- SO4 · Sulfate ion · ion
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 149 | 0.39 | 0.73 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 1883 Ų buried · 32 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 2HCJ · Trypsin-modified Elongation Factor Tu in complex with tetracycline · 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
- Every structure of UniProt P0A6N1
- Elsewhere: RCSB PDB 2HCJ · PDBe 2HCJ · UniProt P0A6N1
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