› 1mt0

X-ray diffraction
2.6Å resolution

ATP-binding domain of hemolysin B from Escherichia coli

Released:
DOI: 10.2210/pdb1mt0/pdb
PDB entry 1mt0 coloured by chain, front view.
PDB entry 1mt0 coloured by chain, side view.
PDB entry 1mt0 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the nucleotide-binding domain of the ABC-transporter haemolysin B: identification of a variable region within ABC helical domains.
Schmitt L, Benabdelhak H, Blight MA, Holland IB, Stubbs MT
J Mol Biol 330 333-42 (2003)
PMID: 12823972

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140359 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-hemolysin translocation ATP-binding protein HlyB Chain: A
Molecule details ›
Chain: A
Length: 241 amino acids
Theoretical weight: 26.92 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P08716 (Residues: 467-707; Coverage: 34%)
Gene name: hlyB
Sequence domains: ABC transporter
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6, null
Spacegroup: P41212
Unit cell:
a: 105.2Å b: 105.2Å c: 125.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.234 0.26
Expression system: Escherichia coli

Quick links

Citations

38 review citations

Structure, function, and evolution of bacterial ATP-binding cassette systems.
Davidson et al. (2008)
37 more

6 mentions without citation

Functional Dynamics Revealed by the Structure of the SufBCD Complex, a Novel ATP-binding Cassette (ABC) Protein That Serves as a Scaffold for Iron-Sulfur Cluster Biogenesis.
Hirabayashi et al. (2015)
5 more