Function and Biology Details
Reaction catalysed:
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Translational (tr)-type GTP-binding domain
- Translation initiation factor 1A (eIF-1A)
- Translation initiation factor IF-2, domain 3 superfamily
- P-loop containing nucleoside triphosphate hydrolase
- Nucleic acid-binding, OB-fold
- RNA-binding domain, S1, IF1 type
- Translation protein, beta-barrel domain superfamily
- Translation initiation factor IF- 2, domain 3
4 more domains
Structure analysis Details
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-153765 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Eukaryotic translation initiation factor 5B
Molecule details ›
Chains: A, B
Length: 606 amino acids
Theoretical weight: 67.72 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 606 amino acids
Theoretical weight: 67.72 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical:
P39730 (Residues: 401-1002; Coverage: 60%)
Sequence domains:
- Elongation factor Tu GTP binding domain
- Translation-initiation factor 2
- Elongation factor Tu domain 4
Eukaryotic translation initiation factor 1A
Molecule details ›
Chain: C
Length: 131 amino acids
Theoretical weight: 15.04 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
Sequence domains: Translation initiation factor 1A / IF-1
Length: 131 amino acids
Theoretical weight: 15.04 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
- Canonical: P38912 (Residues: 27-153; Coverage: 83%)
Sequence domains: Translation initiation factor 1A / IF-1
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SPRING-8 BEAMLINE BL41XU
Spacegroup:
P212121
Expression system: Escherichia coli
