Structure for peptidase C01.032: cathepsin L

Summary Gene structure Alignment Tree Sequences Sequence features Distribution Structure Literature Substrates Pharma

 

PDB Organism Resolution Comment
1CJL Homo sapiens 2.20 Å precursor
Catalytic residues are shown in ball-and-stick representation: Cys138 (engineered to be serine) in yellow, His276 in purple and Asn300 in pink. The propeptide is shown in grey.
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1CS8_P Homo sapiens 1.80 Å procathepsin L
Only the propeptide is shown.
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TERTIARY STRUCTURE DATA
Comment Resolution PDB PDBe SCOP CATH PDBSum Proteopedia Reference
Homo sapiens
precursor 2.20 Å 1CJL 1CJL 1CJL 1CJL 1CJL 1CJL Coulombe et al., 1996
procathepsin L 2.20 Å 1CJL 1CJL 1CJL 1CJL 1CJL 1CJL Coulombe et al., 1996
precursor 1.80 Å 1CS8 1CS8 1CS8 1CS8 1CS8 1CS8
procathepsin L 1.80 Å 1CS8 1CS8 1CS8 1CS8 1CS8 1CS8
complex with MHC class II associated P41 II fragment 2.00 Å 1ICF 1ICF 1ICF 1ICF 1ICF 1ICF Guncar et al., 1999
complex with propeptide-based inhibitor biphenyl-4-yl-acetaldehyde-Cys-D-Arg-Tyr-2-phenylethylamine 1.90 Å 1MHW 1MHW 1MHW 1MHW 1MHW 1MHW Chowdhury et al., 2002
complex with chagasin 1.75 Å 2NQD 2NQD 2NQD 2NQD 2NQD 2NQD Ljunggren et al., 2007
cathsilicatein, a chimera 1.50 Å 2VHS 2VHS 2VHS 2VHS 2VHS 2VHS Fairhead et al., 2008
complex with a nitrile inhibitor 1.45 Å 2XU1 2XU1 2XU1 2XU1 2XU1 2XU1
complex with a nitrile inhibitor 0.90 Å 2XU3 2XU3 2XU3 2XU3 2XU3 2XU3
complex with a nitrile inhibitor 1.12 Å 2XU4 2XU4 2XU4 2XU4 2XU4 2XU4
complex with a nitrile inhibitor 1.60 Å 2XU5 2XU5 2XU5 2XU5 2XU5 2XU5
complex with a nitrile inhibitor 1.15 Å 2YJ2 2YJ2 2YJ2 2YJ2 2YJ2 2YJ2
complex with a nitrile inhibitor 1.30 Å 2YJ8 2YJ8 2YJ8 2YJ8 2YJ8 2YJ8
complex with a nitrile inhibitor 1.35 Å 2YJ9 2YJ9 2YJ9 2YJ9 2YJ9 2YJ9
complex with a nitrile inhibitor 1.40 Å 2YJB 2YJB 2YJB 2YJB 2YJB 2YJB
complex with a nitrile inhibitor 1.14 Å 2YJC 2YJC 2YJC 2YJC 2YJC 2YJC
exploring inhibitor binding at the s subsites of cathepsin l 2.20 Å 3BC3 3BC3 3BC3 3BC3 3BC3 3BC3 Chowdhury et al., 2008
complex with retro-binding inhibitor compound 4 2.50 Å 3H89 3H89 3H89 3H89 3H89 3H89
complex with retro-binding inhibitor compound 9 1.80 Å 3H8B 3H8B 3H8B 3H8B 3H8B 3H8B
complex with retro-binding inhibitor compound 14 2.50 Å 3H8C 3H8C 3H8C 3H8C 3H8C 3H8C
complex with az12878478 1.27 Å 3HHA 3HHA 3HHA 3HHA 3HHA 3HHA
cathepsin l with az13010160 2.33 Å 3HWN 3HWN 3HWN 3HWN 3HWN 3HWN
Cys25Ala mutant 2.20 Å 3IV2 3IV2 3IV2 3IV2 3IV2 3IV2
Cys25Ala mutant; complex with Gln-Leu-Ala peptide 2.50 Å 3K24 3K24 3K24 3K24 3K24 3K24
complex with dipeptidyl glyoxal and diazomethylketone inhibitors 2.20 Å 3OF8 3OF8 3OF8 3OF8 3OF8 3OF8
complex with adiazomethylketone inhibitor 1.76 Å 3OF9 3OF9 3OF9 3OF9 3OF9 3OF9
human cathepsin l apo form with zn 1.92 Å 4AXL 4AXL 4AXL 4AXL 4AXL 4AXL
triazine cathepsin inhibitor complex 2.80 Å 4AXM 4AXM 4AXM 4AXM 4AXM 4AXM
complex with (2s,4r)-4-(2-chloro-4-methoxy- benzenesulfonyl)-1-[3-(5-chloro-pyridin-2-yl)-azetidine-3-carbonyl]- pyrrolidine-2-carboxylic acid (1-cyano-cyclopropyl)-amide 1.43 Å 5F02 5F02 5F02 5F02 5F02 5F02
cleaved cathepsin L bound to the active site of cathepsin L 1.42 Å 5I4H 5I4H 5I4H 5I4H 5I4H 5I4H
complex with (2s,4r)-4-(2-chloro-4-methoxy- benzenesulfonyl)-1-[3-(5-chloro-pyridin-2-yl)-azetidine-3-carbonyl]- pyrrolidine-2-car boxylic acid (1-cyano-cyclopropyl)-amide 1.00 Å 5MAE 5MAE 5MAE 5MAE 5MAE 5MAE
complex with 4-[cyclopentyl(imidazo[1,2-a]pyridin-2- ylmethyl)amino]-6-morpholino-1,3,5-triazine-2-carbonitrile 1.00 Å 5MAJ 5MAJ 5MAJ 5MAJ 5MAJ 5MAJ
complex with 4-[1,3-benzodioxol-5-ylmethyl(2- phenoxyethyl)amino]-5-fluoropyrimidine-2-carbonitrile 1.13 Å 5MQY 5MQY 5MQY 5MQY 5MQY 5MQY
complex with (3s,14e)-19-chloro-n-(1-cyanocyclopropyl)-5-oxo-12,17-dioxa-4-azatricyclo[16.2.2.06,11]docosa-1(21),6(11),7,9, 14,18(22),19-heptaene-3-carboxamide 1.37 Å 6EZP 6EZP 6EZP 6EZP 6EZP 6EZP
complex with (3s,14e)-19-chloro-n-(1-cyanocyclopropyl)-5-oxo-17-oxa-4-azatricyclo[16.2.2.06,11]docosa-1(21),6,8,10,14, 18(22),19-heptaene-3-carboxamide 2.34 Å 6EZX 6EZX 6EZX 6EZX 6EZX 6EZX
complex with (3s,14e)-8-(azetidin-3-yl)-19-chloro-n-(1-cyanocyclopropyl)-5-oxo-12,17-dioxa-4-azatricyclo[16.2.2.06, 11]docosa-1(21),6,8,10,14,18(22),19-heptaene-3-carboxamide 2.02 Å 6F06 6F06 6F06 6F06 6F06 6F06
Mus musculus
theoretical model 0.00 Å 1MVV 1MVV 1MVV 1MVV 1MVV 1MVV