› 1bup

X-ray diffraction
1.7Å resolution

T13S MUTANT OF BOVINE 70 KILODALTON HEAT SHOCK PROTEIN

Released:
DOI: 10.2210/pdb1bup/pdb
PDB entry 1bup coloured by chain, front view.
PDB entry 1bup coloured by chain, side view.
PDB entry 1bup coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change.
Sousa MC, McKay DB
Biochemistry 37 15392-9 (1998)
PMID: 9799500

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
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-148503 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock cognate 71 kDa protein Chain: A
Molecule details ›
Chain: A
Length: 386 amino acids
Theoretical weight: 42.5 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P19120 (Residues: 1-386; Coverage: 59%)
Gene names: HSC70, HSPA8
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand MG 1 x MG
Ligand K 2 x K
Ligand CL 2 x CL
Ligand PO4 1 x PO4
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 143.572Å b: 64.164Å c: 46.236Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.22
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions.
Behnke et al. (2015)
5 more

6 mentions without citation

Hsp70 chaperones: cellular functions and molecular mechanism.
Mayer et al. (2005)
5 more