spacer

PDBe Entry: 1f21 view

DIVALENT METAL COFACTOR BINDING IN THE KINETIC FOLDING TRAJECTORY OF E. COLI RIBONUCLEASE HI
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 1.4 Å, R-factor: 21.7%, Free R-factor: 25.4%, Spacegroup: P 21 21 21
Released 06/12/2000, deposition: 22/05/2000, last revision: 24/02/2009
Authors Goedken, E.R.search; Keck, J.L.search; Berger, J.M.search; Marqusee, S.search
Primary citation Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI.
PROTEIN SCI.search vol:9, pag:1914-1921 (2000) [PubMed ID 11106164 ]search
Keywords RNase Hsearch, nucleasesearch, RNase H*search, ribnuclease Hsearch, metal-binding proteinsearch, protein foldingsearch, HYDROLASEsearch
EC 3.1.26.4 ExPASy BRENDA search (A)
Organism Escherichia coli 562search(A)
UniProt Ribonuclease HI (EC 3.1.26.4) (RNase HI) (Ribonuclease H) (RNase H) P0A7Y4search (A)
Solvent A
Polymers
Id Name Type UniProt Residues Observed
A RIBONUCLEASE HI Protein P0A7Y4 (RNH_ECOLI)search
155 98%
spacer