Brand  (β version)

PDB ID: 1CS8

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Ligands
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Non-standard Residues
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OCS Cysteinesulfonic acid
Glycosylation
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Structure summary

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

DOI: 10.1002/(SICI)1097-0134(19980901)32:4<504::AID-PROT8>3.3.CO;2-Q

Reaction

Chain : A
UniProt : P07711 (CATL1_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
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:37990007, PubMed:9468501
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