Brand  (β version)

PDB ID: 3FNU

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
006 (4r)-3-[(2s,3s)-3-{[(2,6-dimethylphenoxy)acetyl]amino}-2-hydroxy-4-phenylbutanoyl]-N-[(1s,2r)-2-hydroxy-2,3-dihydro-1h-inden-1-yl]-5,5-dimethyl-1,3-thiazolidine-4-carboxamide PoSSuM
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show

Structure summary

Code : 3FNU   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Crystal structure of KNI-10006 bound histo-aspartic protease (HAP) from Plasmodium falciparum
Release Data : 2009-05-12
Compound :
mol_id molecule chains
1 HAP protein A,B,C,D
fragment: Histo-aspartic protease
Source :
mol_id organism_scientific expression_system
1 Plasmodium falciparum  (taxid:36329) Escherichia coli  (taxid:562)
strain: 3D7
gene: HAP, PF14_0078
expression_system_strain: Rosetta-gami B (DE3)pLysS
expression_system_vector_type: Plasmid
expression_system_plasmid: pET32b(+)
Authors : Bhaumik, P., Gustchina, A., Wlodawer, A.
Keywords : Histo-aspartic protease, HYDROLASE, Plasmepsin, Aspartic protease, KNI, KNI-10006, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 3.00 Å )
Citation :

Crystal structures of the histo-aspartic protease (HAP) from Plasmodium falciparum.

Bhaumik, P.,Xiao, H.,Parr, C.L.  et al.
(2009)  J.Mol.Biol.  388 : 520 - 540

PubMed: 19285084
DOI: 10.1016/j.jmb.2009.03.011

Reaction

Chain : A, B, C, D
UniProt : Q8IM15 (PLM3_PLAF7)
Reaction: EC: Evidence:
Physiological Direction:
Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves small molecules substrates such as Ala-Leu-Glu-Arg-Thr-Phe-|-Phe(NO2)-Ser-Phe-Pro-Thr. 3.4.23.39 PubMed:16624575, PubMed:18312598, PubMed:20435072
-