5aqu

X-ray diffraction
1.92Å resolution

Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues

Released:

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Heat shock cognate 71 kDa protein Chain: A
Molecule details ›
Chain: A
Length: 386 amino acids
Theoretical weight: 42.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P11142 (Residues: 1-381; Coverage: 59%)
Gene names: HSC70, HSP73, HSPA10, HSPA8
Structure domains:
BAG family molecular chaperone regulator 1 Chain: B
Molecule details ›
Chain: B
Length: 118 amino acids
Theoretical weight: 13.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q99933 (Residues: 222-334; Coverage: 33%)
Gene names: BAG1, HAP
Sequence domains: BAG domain
Structure domains: BAG domain

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: C2
Unit cell:
a: 114.024Å b: 40.7Å c: 127.421Å
α: 90° β: 114.26° γ: 90°
R-values:
R R work R free
0.179 0.178 0.201
Expression system: Escherichia coli BL21