Function and Biology Details
Reaction catalysed:
dGTP + H(2)O = deoxyguanosine + triphosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Translational (tr)-type GTP-binding domain
- P-loop containing nucleoside triphosphate hydrolase
- Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal
- Translation elongation factor EFTu/EF1A, C-terminal
- Translation elongation factor EFTu-like, domain 2
- Elongation factor Tu, domain 2
- Translation protein, beta-barrel domain superfamily
- Tr-type G domain, conserved site
3 more domains
Structure domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Elongation factor Tu-B and Thiocillin GE2270 (preferred)
PDBe Complex ID:
PDB-CPX-158000 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Elongation factor Tu-B
Molecule details ›
Chain: A
Length: 405 amino acids
Theoretical weight: 44.73 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 405 amino acids
Theoretical weight: 44.73 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P60339 (Residues: 2-406; Coverage: 100%)
Sequence domains:
- Elongation factor Tu GTP binding domain
- Elongation factor Tu domain 2
- Elongation factor Tu C-terminal domain
Thiocillin GE2270
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.48 KDa
Source organism: Planobispora rosea
UniProt:
Length: 15 amino acids
Theoretical weight: 1.48 KDa
Source organism: Planobispora rosea
UniProt:
- Canonical: Q7M0J8 (Residues: 1-14; Coverage: 100%)
