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Ligands
Code Name Style Show Link
0ZL N-(ethoxycarbonyl)-L-leucyl-N-[(1r,2s,3s)-1-(cyclohexylmethyl)-2,3-dihydroxy-5-methylhexyl]-L-leucinamide
Non-standard Residues
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Glycosylation
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Code : 1PSA   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/hydrolase inhibitor
Title : STRUCTURE OF A PEPSIN(SLASH)RENIN INHIBITOR COMPLEX REVEALS A NOVEL CRYSTAL PACKING INDUCED BY MINOR CHEMICAL ALTERATIONS IN THE INHIBITOR
Release Data : 1994-01-31
Compound :
mol_id molecule chains
1 PEPSIN A A,B
ec: 3.4.23.1
Source :
mol_id organism_scientific organism_common
1 Sus scrofa  (taxid:9823) Pig
Authors : Chen, L., Abad-Zapatero, C.
Keywords : ACID PROTEINASE, HYDROLASE-hydrolase inhibitor complex
Exp. method : X-RAY DIFFRACTION ( 2.9 Å )
Citation :

Structure of a pepsin/renin inhibitor complex reveals a novel crystal packing induced by minor chemical alterations in the inhibitor.

Chen, L.,Erickson, J.W.,Rydel, T.J.  et al.
(1992)  Acta Crystallogr.,Sect.B  48 : 476 - 488

PubMed: 1418819
DOI: 10.1107/S0108768192001939

Inhibitor Binding Induces Structural Changes in Porcine Pepsin

Abad-Zapatero, C.,Rydel, T.J.,Neidhart, D.J.  et al.
(1991)  Adv.Exp.Med.Biol.  306 : 9

Revised 2.3 Angstroms Structure of Porcine Pepsin: Evidence for a Flexible Subdomain

Abad-Zapatero, C.,Rydel, T.J.,Erickson, J.
(1990)  Proteins  8 : 62

Chain : A, B
UniProt : P00791 (PEPA_PIG)
Reaction: EC: Evidence:
Physiological Direction:
Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His- 5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu- 17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin. 3.4.23.1 PROSITE- ProRule:PRU10094
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