Brand  (β version)

PDB ID: 1FQ6

Hetero Atom Contents

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
0QF N-[(1s)-2-{[(2s,3r,4s)-1-cyclohexyl-3,4-dihydroxy-6-methylheptan-2-yl]amino}-1-(ethylsulfanyl)-2-oxoethyl]-nalpha-(morpholin-4-ylsulfonyl)-L-phenylalaninamide PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
BMA Beta-D-mannopyranose
GUP Alpha-L-gulopyranose
NAG 2-acetamido-2-deoxy-beta-D-glucopyranose
Modification
Code Name Show

Structure summary

Code : 1FQ6   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : X-RAY STRUCTURE OF GLYCOL INHIBITOR PD-133,450 BOUND TO SACCHAROPEPSIN
Release Data : 2000-09-20
Compound :
mol_id molecule chains synonym
1 SACCHAROPEPSIN A ASPARTATE PROTEASE, PROTEINASE A
ec: 3.4.23.25
Source :
mol_id organism_scientific organism_common
1 Saccharomyces cerevisiae  (taxid:4932) Baker's yeast
Authors : Cronin, N.B., Badasso, M.O., Tickle, I.J., Dreyer, T., Hoover, D.J., Rosati, R.L., Humblet, C.C., Lunney, E.A., Cooper, J.B.
Keywords : HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.7 Å )
Citation :

X-ray structures of five renin inhibitors bound to saccharopepsin: exploration of active-site specificity.

Cronin, N.B.,Badasso, M.O.,J Tickle, I.  et al.
(2000)  J.Mol.Biol.  303 : 745 - 760

PubMed: 11061973
DOI: 10.1006/jmbi.2000.4181

The Three-dimensional Structure at 2.4 A Resolution of Glycosylated Proteinase A from the Lysosome-like Vacuole of Saccharomyces cerevisiae

Aguilar, C.F.,Cronin, N.B.,Badasso, M.  et al.
(1997)  J.Mol.Biol.  267 : 899 - 915

DOI: 10.1006/jmbi.1996.0880

Reaction

Chain : A
UniProt : P07267 (CARP_YEAST)
Reaction: EC: Evidence:
Physiological Direction:
Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg. 3.4.23.25 -
-