› 1no5

X-ray diffraction
1.8Å resolution

Structure of HI0073 from Haemophilus influenzae, the nucleotide binding domain of the HI0073/HI0074 two protein nucleotidyl transferase.

Released:
DOI: 10.2210/pdb1no5/pdb
PDB entry 1no5 coloured by chain, front view.
PDB entry 1no5 coloured by chain, side view.
PDB entry 1no5 coloured by chain, top view.
Source organism: Haemophilus influenzae
Primary publication:
Structure of HI0073 from Haemophilus influenzae, the nucleotide-binding domain of a two-protein nucleotidyl transferase.
Lehmann C, Pullalarevu S, Krajewski W, Willis MA, Galkin A, Howard A, Herzberg O
Proteins 60 807-11 (2005)
PMID: 16028221

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assemblies composition:
monomeric
homo hexamer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155159 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Probable protein adenylyltransferase MntA Chains: A, B
Molecule details ›
Chains: A, B
Length: 114 amino acids
Theoretical weight: 13.2 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: P43933 (Residues: 1-114; Coverage: 100%)
Gene names: HI_0073, mntA
Sequence domains: Nucleotidyltransferase domain
Structure domains: Beta Polymerase, domain 2

Ligands and Environments

4 bound ligands:
Ligand ZN 8 x ZN
Ligand GOL 1 x GOL
Ligand SO4 2 x SO4
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-BM
Spacegroup: P63
Unit cell:
a: 89.56Å b: 89.56Å c: 61.48Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 0.2 0.282
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Global gene expression mediated by Thermus thermophilus SdrP, a CRP/FNR family transcriptional regulator.
Agari et al. (2008)
3 more

10 mentions without citation

RNA-specific ribonucleotidyl transferases.
Martin et al. (2007)
9 more