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PDBsum entry 3s2o

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protein ligands metals links
Hydrolase/hydrolase inhibitor PDB id
3s2o
Jmol
Contents
Protein chain
378 a.a.
Ligands
EV6
Metals
IOD ×2
Waters ×69
PDB id:
3s2o
Name: Hydrolase/hydrolase inhibitor
Title: Fragment based discovery and optimisation of bace-1 inhibito
Structure: Beta-secretase 1. Chain: a. Fragment: unp residues 46-453. Synonym: aspartyl protease 2, asp2, asp 2, beta-site amyloi precursor protein cleaving enzyme 1, beta-site app cleaving memapsin-2, membrane-associated aspartic protease 2. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: bace, bace1, kiaa1149. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.60Å     R-factor:   0.208     R-free:   0.261
Authors: J.Madden,R.Godemann,M.A.Smith,D.Hallett,J.Barker,J.Kraemer
Key ref: J.Madden et al. (2010). Fragment-based discovery and optimization of BACE1 inhibitors. Bioorg Med Chem Lett, 20, 5329-5333. PubMed id: 20656487 DOI: 10.1016/j.bmcl.2010.06.089
Date:
17-May-11     Release date:   01-Jun-11    
Supersedes: 3msm
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P56817  (BACE1_HUMAN) -  Beta-secretase 1
Seq:
Struc:
501 a.a.
378 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.4.23.46  - Memapsin 2.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     proteolysis   1 term 
  Biochemical function     aspartic-type endopeptidase activity     1 term  

 

 
DOI no: 10.1016/j.bmcl.2010.06.089 Bioorg Med Chem Lett 20:5329-5333 (2010)
PubMed id: 20656487  
 
 
Fragment-based discovery and optimization of BACE1 inhibitors.
J.Madden, J.R.Dod, R.Godemann, J.Kraemer, M.Smith, M.Biniszkiewicz, D.J.Hallett, J.Barker, J.D.Dyekjaer, T.Hesterkamp.
 
  ABSTRACT  
 
No abstract given.