spacer

PDBe Entry: 1ngi view

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
Summary
Header HYDROLASE(ACTING ON ACID ANHYDRIDES)search
Method X-RAY DIFFRACTION
Experiment Resolution: 2.15 Å, R-factor: 20.0%, Spacegroup: P 21 21 21
Released 31/08/1994, deposition: 17/05/1994, last revision: 24/02/2009
Authors Flaherty, K.M.search; Wilbanks, S.M.search; Deluca-Flaherty, C.search; Mckay, D.B.search
Primary citation 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.
J.BIOL.CHEM.search vol:269, pag:12899-12907 (1994) [PubMed ID 8175707 ]search
Keywords HYDROLASE(ACTING ON ACID ANHYDRIDES)search
Organism Bos taurus(cattle) 9913search(A)
UniProt Heat shock cognate 71 kDa protein (Heat shock 70 kDa protein 8) P19120search (A)
Solvent A
Polymers
Id Name Type UniProt Residues Observed
A HEAT-SHOCK COGNATE 70 kD PROTEIN Protein P19120 (HSP7C_BOVIN)search
386 97%
Heterogens
Id Name Ligands
A CALCIUM ION CA search
A PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER ANP search
spacer