Brand  (β version)

color scheme of protein:

hetatm:

x
information
centroid:
interaction residue:

chain:

Ligands
Code Name Link
0GM N-[(5s,9s,10s,13s)-9-hydroxy-5,10-bis(2-methylpropyl)-4,7,12,16-tetraoxo-3,6,11,17-tetraazabicyclo[17.3.1]tricosa-1(23),19,21-trien-13-yl]-3-(naphthalen-1-yl)-2-(naphthalen-1-ylmethyl)propanamide
SO4 Sulfate ion
Modified Residues
Code Name Link
SUI (3-amino-2,5-dioxo-1-pyrrolidinyl)acetic acid
Code : 1GVV   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Five Atomic Resolution Structures of Endothiapepsin Inhibitor Complexes; implications for the Aspartic Proteinase Mechanism
Release Data : 2002-07-04
Compound :
mol_id molecule chains synonym
1 ENDOTHIAPEPSIN A ASPARTATE PROTEASE
ec: 3.4.23.22
Source :
mol_id organism_scientific organism_common
1 ENDOTHIA PARASITICA  (taxid:5116) CHESTNUT BLIGHT FUNGUS
Authors : Coates, L., Erskine, P.T., Crump, M.P., Wood, S.P., Cooper, J.B.
Keywords : HYDROLASE-HYDROLASE INHIBITOR COMPLEX, ASPARTIC PROTEINASE MECHANISM, Z TETRAHEDRAL INTERMEDIATE, HYDROLASE- HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 1.05 Å )
Citation :

Five Atomic Resolution Structures of Endothiapepsin Inhibitor Complexes: Implications for the Aspartic Proteinase Mechanism

Coates, L.,Erskine, P.T.,Crump, M.P.  et al.
(2002)  J.Mol.Biol.  318 : 1405

PubMed: 12083527
DOI: 10.1016/S0022-2836(02)00197-3

Chain : A
UniProt : P11838 (CARP_CRYPA)
Reaction : Reaction=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.; EC=3.4.23.22;