Brand  (β version)

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Modified Residues
Code Name Link
0HQ Diazomethane
PHQ Benzyl chlorocarbonate
Code : 1KHP   PDBj   RCSB PDB   PDBe
Header : HYDROLASE/HYDROLASE INHIBITOR
Title : Monoclinic form of papain/ZLFG-DAM covalent complex
Release Data : 2003-09-09
Compound :
mol_id molecule chains synonym
1 Papain A Papaya proteinase I, PPI
ec: 3.4.22.2
fragment: Papain, Residues 134-345
mol_id molecule chains
2 peptidic inhibitor I
Source :
mol_id organism_scientific organism_common
1 Carica papaya  (taxid:3649) Papaya
mol_id organism_scientific
2
synthetic: yes
Authors : Janowski, R., Kozak, M., Jankowska, E., Grzonka, Z., Jaskolski, M.
Keywords : PROTEASE INHIBITOR, DIAZOMETHYLKETONE INHIBITOR, IRREVERSIBLE INHIBITOR, HYDROLASE-HYDROLASE INHIBITOR COMPLEX
Exp. method : X-RAY DIFFRACTION ( 2.0 Å )
Citation :

Two polymorphs of a covalent complex between papain and a diazomethylketone inhibitor

Janowski, R.,Kozak, M.,Jankowska, E.  et al.
(2004)  J.Pept.Res.  64 : 141 - 150

PubMed: 15357669
DOI: 10.1111/j.1399-3011.2004.00181.x

Crystallization and preliminary crystallographic studies of a new crystal form of papain from Carica papaya.

Kozak, M.,Kozian, E.,Grzonka, Z.  et al.
(1997)  ACTA BIOCHIM.POL.  44 : 601 - 605

Structural studies of cysteine proteases and their inhibitors

Grzonka, Z.,Jankowska, E.,Wieczerzak, E.  et al.
(2001)  ACTA BIOCHIM.POL.  48 : 1 - 20

Binding of chloromethyl ketone substrate analogues to crystalline papain.

Drenth, J.,Kalk, K.H.,Swen, H.M.
(1976)  Biochemistry  15 : 3731 - 3738

Structure of monoclinic papain at 1.60 Angstroms resolution.

Pickersgill, R.W.,Harris, G.W.,Garman, E.
(1992)  ACTA CRYSTALLOGR.,SECT.B  48 : 59 - 66

DOI: 10.1107/S0108768191006572

Binding modes of a new epoxysuccinyl-peptide inhibitor of cysteine proteases. Where and how do cysteine proteases express their selectivity?

Czaplewski, C.,Grzonka, Z.,Jaskolski, M.  et al.
(1999)  BIOCHIM.BIOPHYS.ACTA  1431 : 290 - 305

DOI: 10.1016/S0167-4838(99)00053-9

Chain : A
UniProt : P00784 (PAPA1_CARPA)
Reaction : Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'.; EC=3.4.22.2;