Function and Biology Details
Reaction catalysed:
NAD(+) + diphthamide-[translation elongation factor 2] = nicotinamide + N-(ADP-D-ribosyl)diphthamide-[translation elongation factor 2]
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Translational (tr)-type GTP-binding domain
- Exotoxin A catalytic domain
- Elongation factor EFG, domain V-like
- Translation elongation factor EFG/EF2, domain IV
- EF-G domain III/V-like
- P-loop containing nucleoside triphosphate hydrolase
- Small ribosomal subunit protein uS5 domain 2-type fold, subgroup
- Ribosomal protein uS5 domain 2-type superfamily
5 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Exotoxin A and Elongation factor 2 (preferred)
PDBe Complex ID:
PDB-CPX-145827 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Elongation factor 2
Molecule details ›
Chains: A, C, E
Length: 842 amino acids
Theoretical weight: 93.55 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
Sequence domains:
Length: 842 amino acids
Theoretical weight: 93.55 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
- Canonical:
P32324 (Residues: 1-842; Coverage: 100%)
Sequence domains:
- Elongation factor Tu GTP binding domain
- Elongation factor Tu domain 2
- Elongation Factor G, domain III
- Elongation factor G, domain IV
- Elongation factor G C-terminus
Exotoxin A
Molecule details ›
Chains: B, D, F
Length: 207 amino acids
Theoretical weight: 22.5 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
Sequence domains: Exotoxin A catalytic
Structure domains: Diphtheria Toxin, domain 1
Length: 207 amino acids
Theoretical weight: 22.5 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
- Canonical: P11439 (Residues: 424-630; Coverage: 34%)
Sequence domains: Exotoxin A catalytic
Structure domains: Diphtheria Toxin, domain 1
