› 5fpn

X-ray diffraction
1.96Å resolution

Structure of heat shock-related 70kDA protein 2 with small-molecule ligand 3,5-dimethyl-1H-pyrazole-4-carboxylic acid (AT9084) in an alternate binding site.

Released:
DOI: 10.2210/pdb5fpn/pdb
PDB entry 5fpn coloured by chain, front view.
PDB entry 5fpn coloured by chain, side view.
PDB entry 5fpn coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Detection of secondary binding sites in proteins using fragment screening.
Ludlow RF, Verdonk ML, Saini HK, Tickle IJ, Jhoti H
Proc Natl Acad Sci U S A 112 15910-5 (2015)
PMID: 26655740

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157070 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock-related 70 kDa protein 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 640 amino acids
Theoretical weight: 70.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P54652 (Residues: 4-639; Coverage: 100%)
Gene name: HSPA2
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand KYD 4 x KYD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P21
Unit cell:
a: 48.82Å b: 94.85Å c: 81.87Å
α: 90° β: 90.15° γ: 90°
R-values:
R R work R free
0.177 0.174 0.232
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Twenty years on: the impact of fragments on drug discovery.
Erlanson et al. (2016)
10 more

3 mentions without citation

The remarkable multivalency of the Hsp70 chaperones.
Zuiderweg et al. (2017)
2 more