Research workbench
Elongation factor tu in complex with aurodox
Analyse Elongation factor tu in complex with aurodox in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HA3
- Type
- protein
- Length
- 770 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor tu
- EC
- 3.1.5.1
- UniProt
- P07157
- Ligands
- GDP, MAU, MG
- Pockets
- 5 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor tu (EC 3.1.5.1) | protein | 391 | 23% helix, 36% strand | P07157 |
| B | Elongation factor tu (EC 3.1.5.1) | protein | 379 | 23% helix, 37% strand | P07157 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
- MAU · N-methyl kirromycin · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- BME · Beta-mercaptoethanol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 712 | 0.81 | 0.85 | 76 | empty |
| 2 | 754 | 0.76 | 0.80 | 91 | GDP, MG, MAU, BME |
| 3 | 586 | 0.71 | 0.80 | 67 | MAU, BME |
| 4 | 55 | 0.31 | 0.76 | 16 | empty |
| 5 | 54 | 0.30 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1099 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (additive adduct).
Compared structures
- 1HA3 · ELONGATION FACTOR TU IN COMPLEX WITH aurodox · 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 P07157
- Elsewhere: RCSB PDB 1HA3 · PDBe 1HA3 · UniProt P07157
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