Brand  (β version)

PDB ID: 3ER3

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Ligands
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0EL 6-ammonio-N-[(2r,4r,5r)-5-{[N-(tert-butoxycarbonyl)-L-phenylalanyl-3-(1h-imidazol-3-ium-4-yl)-L-alanyl]amino}-6-cyclohexyl-4-hydroxy-2-(2-methylpropyl)hexanoyl]-L-norleucylphenylalanine PoSSuM
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Structure summary

Code : 3ER3   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : The active site of aspartic proteinases
Release Data : 1991-04-15
Compound :
mol_id molecule chains
1 ENDOTHIAPEPSIN E
ec: 3.4.23.6
Source :
mol_id organism_scientific organism_common
1 Cryphonectria parasitica  (taxid:5116) Chestnut blight fungus
Authors : Al-Karadaghi, S., Cooper, J.B., Veerapandian, B., Hoover, D., Blundell, T.L.
Keywords : ACID PROTEINASE, HYDROLASE-HYDROLASE INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.0 Å )
Citation :

The Active Site of Aspartic Proteinases

Pearl, L.,Blundell, T.
(1984)  FEBS Lett.  174 : 96 - 101

PubMed: 6381096
DOI: 10.1016/0014-5793(84)81085-6

Active Site of Acid Proteinases

Blundell, T.L.,Jones, H.B.,Khan, G.  et al.
(1979)  Proc.FEBS Meet.  60 : 281

The Three-Dimensional Structure of Acid Proteinases

Blundell, T.L.,Jenkins, J.A.,Khan, G.  et al.
(1979)  Proc.FEBS Meet.  52 : 81

Four-Fold Structural Repeat in the Acid Proteases

Blundell, T.L.,Sewell, B.T.,Mclachlan, A.D.
(1979)  Biochim.Biophys.Acta  580 : 24

Structural Evidence for Gene Duplication in the Evolution of Acid Proteases

Tang, J.,James, M.N.G.,Hsu, I.N.  et al.
(1978)  Nature  271 : 618

Homology Among Acid Proteases. Comparison of Crystal Structures at 3 Angstroms Resolution of Acid Proteases from Rhizopus Chinensis and Endothia Parasitica

Subramanian, E.,Swan, I.D.A.,Liu, M.  et al.
(1977)  Proc.Natl.Acad.Sci.USA  74 : 556

X-Ray Analysis and Circular Dichroism of the Acid Protease from Endothia Parasitica and Chymosin

Jenkins, J.,Tickle, I.,Sewell, T.  et al.
(1977)  Adv.Exp.Med.Biol.  95 : 43

Reaction

Chain : E
UniProt : P11838 (CARP_CRYPA)
Reaction: EC: Evidence:
Physiological Direction:
Hydrolysis of proteins with specificity similar to that of pepsin A, prefers hydrophobic residues at P1 and P1', but does not cleave 14-Ala-|-Leu-15 in the B chain of insulin or Z-Glu-Tyr. Clots milk. 3.4.23.22 -
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