Structure of PDB 2yjc Chain A

Receptor sequence
>2yjcA (length=219) Species: 9606 (Homo sapiens) [Search protein sequence]
APRSVDWREKGYVTPVKNQGQCGSCWAFSATGALEGQMFRKTGRLISLSE
QNLVDCSGPQGNEGCNGGLMDYAFQYVQDNGGLDSEESYPYEATEESCKY
NPKYSVANDTGFVDIPKQEKALMKAVATVGPISVAIDAGHESFLFYKEGI
YFEPDCSSEDMDHGVLVVGYGFESTSDNNKYWLVKNSWGEEWGMGGYVKM
AKDRRNHCGIASAASYPTV
3D structure
PDB2yjc Halogen Bonding at the Active Sites of Human Cathepsin L and Mek1 Kinase: Efficient Interactions in Different Environments.
ChainA
Resolution1.14 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q19 C25 H163 N187
Catalytic site (residue number reindexed from 1) Q19 C25 H163 N186
Enzyme Commision number 3.4.22.15: cathepsin L.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 424 A G23 C25 E63 G67 G68 L69 M70 A135 M161 D162 H163 G23 C25 E63 G67 G68 L69 M70 A135 M161 D162 H163 PDBbind-CN: -logKd/Ki=7.66,IC50=0.022uM
Gene Ontology
Molecular Function
GO:0008234 cysteine-type peptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:2yjc, PDBe:2yjc, PDBj:2yjc
PDBsum2yjc
PubMed21898833
UniProtP07711|CATL1_HUMAN Procathepsin L (Gene Name=CTSL)

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