spacer
EBI PDBe PDBeView

PDBe Entry: 1qf0 view

THERMOLYSIN (E.C.3.4.24.27) COMPLEXED WITH (2-SULPHANYL-3-PHENYLPROPANOYL)-PHE-TYR. PARAMETERS FOR ZN-BIDENTATION OF MERCAPTOACYLDIPEPTIDES IN METALLOENDOPEPTIDASE
Summary
Header HYDROLASEsearch
Method X-RAY DIFFRACTION
Experiment Resolution: 2.2 Å, R-factor: 16.1%, Free R-factor: 21.6%, Spacegroup: P 61 2 2
Released 29/12/1999, deposition: 06/04/1999, last revision: 24/02/2009
Authors Gaucher, J.-F.search; Selkti, M.search; Tiraboschi, G.search; Prange, T.search; Roques, B.P.search; Tomas, A.search; Fournie-Zaluski, M.C.search
Primary citation Crystal structures of alpha-mercaptoacyldipeptides in the thermolysin active site: structural parameters for a Zn monodentation or bidentation in metalloendopeptidases.
BIOCHEMISTRYsearch vol:38, pag:12569-12576 (1999) [PubMed ID 10504225 ]search
Keywords NEUTRAL ENDOPEPTIDASEsearch, ZN METALLOPEPTIDASEsearch, HYDROLASEsearch
EC 3.4.24.27 ExPASy BRENDA search (A)
Organism Bacillus thermoproteolyticus 1427search(A)
UniProt Thermolysin precursor (EC 3.4.24.27) (Thermostable neutral proteinase) P00800search (A)
Solvent A
Polymers
Id Name Type UniProt Residues Observed
A PROTEIN (THERMOLYSIN) Protein P00800 (THER_BACTH)search
 316 100%
Heterogens
Id Name Ligands
A ZINC ION ZN search
A CALCIUM ION CA search
A (2-SULFANYL-3-PHENYLPROPANOYL)-PHE-TYR TI2 search
A DIMETHYL SULFOXIDE DMS search
spacer