Structure of PDB 1tl9 Chain A

Receptor sequence
>1tl9A (length=321) Species: 10116 (Rattus norvegicus) [Search protein sequence]
NAIKYLGQDYENLRARCLQNGVLFQDDAFPPVSHSLGFKELGPNSSKTYG
IKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNETILH
RVVPYGQSFQEGYAGIFHFQLWQFGEWVDVVVDDLLPTKDGKLVFVHSAQ
GNEFWSALLEKAYAKVNGSYEALSGGCTSEAFEDFTGGVTEWYDLQKAPS
DLYQIILKALERGSLLGCSINISDIRDLEAITFKNLVRGHAYSVTDAKQV
TYQGQRVNLIRMRNPWGEVEWKGPWSDNSYEWNKVDPYEREQLRVKMEDG
EFWMSFRDFIREFTKLEICNL
3D structure
PDB1tl9 Crystal Structures of Calpain-E64 and -Leupeptin Inhibitor Complexes Reveal Mobile Loops Gating the Active Site
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) Q109 C115 H272 N296 W298
Catalytic site (residue number reindexed from 1) Q77 C83 H240 N264 W266
Enzyme Commision number 3.4.22.52: calpain-1.
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 peptide A E72 G113 C115 G207 G208 S251 E261 G271 E40 G81 C83 G175 G176 S219 E229 G239
BS02 CA A V99 G101 D106 E185 V67 G69 D74 E153
BS03 CA A E302 D309 M329 D331 E333 E270 D277 M297 D299 E301
Gene Ontology
Molecular Function
GO:0004198 calcium-dependent cysteine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1tl9, PDBe:1tl9, PDBj:1tl9
PDBsum1tl9
PubMed15491615
UniProtP97571|CAN1_RAT Calpain-1 catalytic subunit (Gene Name=Capn1)

[Back to BioLiP]