› 1ngb

X-ray diffraction
2.18Å resolution

STRUCTURAL BASIS OF THE 70-KILODALTON HEAT SHOCK COGNATE PROTEIN ATP HYDROLYTIC ACTIVITY, II. STRUCTURE OF THE ACTIVE SITE WITH ADP OR ATP BOUND TO WILD TYPE AND MUTANT ATPASE FRAGMENT

Released:
DOI: 10.2210/pdb1ngb/pdb
PDB entry 1ngb coloured by chain, front view.
PDB entry 1ngb coloured by chain, side view.
PDB entry 1ngb coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment.
Flaherty KM, Wilbanks SM, DeLuca-Flaherty C, McKay DB
J Biol Chem 269 12899-907 (1994)
PMID: 8175707

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: 42.51 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P19120 (Residues: 1-386; Coverage: 59%)
Gene names: HSC70, HSPA8
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 1 x MG
Ligand PO4 1 x PO4
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 145.3Å b: 65Å c: 46.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 not available
Expression system: Not provided

Quick links

Citations

10 review citations

The Hsp70 and Hsp60 chaperone machines.
Bukau et al. (1998)
9 more