Eukaryotic translation initiation factor 5A-1
Homo sapiens
State in the Current Structure
| Assembly | Oligomeric State | Construct | Mutations and Modifications | Ligands, Ions and Associated Components | Method and Experimental Conditions | Structure Quality |
|---|---|---|---|---|---|---|
| 1 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count | Chain A; UniProt 15–151 | Fragment:Residues 15-151 | UNX UNKNOWN LIGAND × 6 | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;22% PEG 3350, 0.2M Ammonium sulfate, 0.1M Sodium cacodylate. Cryoprotected with 20% PEG 3350 and 20% Ethylene glycol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K | Resolution 2.50 Å R-free 0.300 |
| 2 | Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count | Chain B; UniProt 15–151 | Fragment:Residues 15-151 | No other associated polymer | X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5.5;291 K;22% PEG 3350, 0.2M Ammonium sulfate, 0.1M Sodium cacodylate. Cryoprotected with 20% PEG 3350 and 20% Ethylene glycol, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K | Resolution 2.50 Å R-free 0.300 |
Other States of the Same Protein in the Database
Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.
2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states
View Construct and Data Evidence
| UniProt name | IF5A1_HUMAN |
| Isoform | — |
| PDB entities | 1 |
| Chains and sequence ranges | Author chain A; PDBConstruct 2–138; UniProt 15–151 Author chain B; PDBConstruct 2–138; UniProt 15–151 |