Het-PDB Navi2 (PDB: 1CS8)

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Ligands
Code	Name		Style	Show	Link

Non-standard Residues
Code	Name	Show
OCS	Cysteinesulfonic acid

Glycosylation
Code	Name	Emphasize

Modification
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Download interaction data: 1CS8

Code :

1CS8 PDBj RCSB PDB PDBe

Header :

HYDROLASE

Title :

CRYSTAL STRUCTURE OF PROCATHEPSIN L

Release Data :

1999-08-23

Compound :

mol_id	molecule	chains
1	HUMAN PROCATHEPSIN L	A
	ec: 3.4.22.15 mutation: T110A

Source :

mol_id	organism_scientific	organism_common	expression_system
1	Homo sapiens (taxid:9606)	Human	Pichia pastoris (taxid:4922)
	expression_system_plasmid: PPIC9

Authors :

Cygler, M., Coulombe, R.

Keywords :

PROSEGMENT, PROPEPTIDE, INHIBITION, HYDROLASE

Exp. method :

X-RAY DIFFRACTION ( 1.8 Å )

Citation :

Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment.

Coulombe, R.,Grochulski, P.,Sivaraman, J. et al.
(1996) EMBO J. 15 : 5492 - 5503

PubMed: 8896443

Structural Basis for Specificity of Papain-Like Cysteine Protease Proregions Toward Their Cognate Enzymes

Groves, M.R.,Coulombe, R.,Jenkins, J. et al.
(1998) Proteins 32 : 504 - 514

Chain :

UniProt :

P07711 (CATL1_HUMAN)

Reaction:	EC:	Evidence:
Reaction:	Physiological Direction:	Evidence:
Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl- dipeptidase activity.	3.4.22.15	PubMed:9468501
	-	PubMed:9468501

PDB ID: 1CS8