Research workbench
Crystal structure of Acinetobacter baumannii DsbA in complex with EF-Tu
Analyse Crystal structure of Acinetobacter baumannii DsbA in complex with EF-Tu in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4P3Y
- Type
- protein
- Length
- 567 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.154
- Source
- Acinetobacter baumannii AYE; Escherichia coli BL21(DE3)
- Molecule
- Elongation factor Tu 1; Thiol:disulfide interchange protein
- UniProt
- P0CE47, B0V5X3
- Ligands
- GDP, MG
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · resolution 2.154 · 2 distinct chains · 32% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor Tu 1 | protein | 386 | 24% helix, 37% strand | P0CE47 |
| B | Thiol:disulfide interchange protein | protein | 181 | 50% helix, 12% strand | B0V5X3 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- GOL · Glycerol · additive · 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1114 | 0.75 | 0.78 | 83 | empty |
| 2 | 153 | 0.55 | 0.81 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 899 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 4P3Y · Crystal structure of acinetobacter baumannii dsba in complex with ef- tu · the same entry in another collection · chain A against A, TM-score 1.00
- P0CE47 · AlphaFold monomer V2.0 prediction for elongation factor tu 1 (P0CE47) · a predicted model of the same protein · chain A against A, TM-score 0.56
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 P0CE47
- Every structure of UniProt B0V5X3
- Elsewhere: RCSB PDB 4P3Y · PDBe 4P3Y · UniProt P0CE47 · UniProt B0V5X3
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