Het-PDB Navi2 (PDB: 1KHQ)

The number of atoms exceeds 100,000.
So, it can not be displayed here.

Select unit:

Select chain: Sequence Hide other chain(s)

Data format:

Color scheme of protein:

Ligands
Code	Name		Style	Show	Link

Non-standard Residues
Code	Name	Show

Glycosylation
Code	Name	Emphasize

Modification
Code	Name	Show
0HQ	Diazomethane
PHQ	Benzyl chlorocarbonate

Download interaction data: 1KHQ

Code :

1KHQ PDBj RCSB PDB PDBe

Header :

HYDROLASE/HYDROLASE INHIBITOR

Title :

ORTHORHOMBIC 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 ( 1.6 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 :

UniProt :

P00784 (PAPA1_CARPA)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
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'.	3.4.22.2	PubMed:21416241, PubMed:23151624, PubMed:2404797
	-	PubMed:21416241, PubMed:23151624, PubMed:2404797

PDB ID: 1KHQ

Hetero Atom Contents

Structure summary

Reaction