› 2pmk

X-ray diffraction
1.6Å resolution

Crystal structures of an isolated ABC-ATPase in complex with TNP-ADP

Released:
DOI: 10.2210/pdb2pmk/pdb
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PDB entry 2pmk coloured by chain, front view.
PDB entry 2pmk coloured by chain, side view.
PDB entry 2pmk coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Water-mediated protein-fluorophore interactions modulate the affinity of an ABC-ATPase/TNP-ADP complex.
Oswald C, Jenewein S, Smits SH, Holland IB, Schmitt L
J Struct Biol 162 85-93 (2008)
PMID: 18155559

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: 243 amino acids
Theoretical weight: 27.2 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
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

2 bound ligands:
Ligand 128 1 x 128
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MPG/DESY, HAMBURG BEAMLINE BW6
Spacegroup: C2
Unit cell:
a: 179.682Å b: 34.648Å c: 38.293Å
α: 90° β: 98.07° γ: 90°
R-values:
R R work R free
0.193 0.192 0.223
Expression system: Escherichia coli BL21(DE3)

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Citations

3 citation in other articles

Specific lipids modulate the transporter associated with antigen processing (TAP).
Schölz et al. (2011)
2 more

3 mentions without citation

Trinitrophenyl derivatives bind differently from parent adenine nucleotides to Ca2+-ATPase in the absence of Ca2+.
Toyoshima et al. (2011)
2 more

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