Structure of PDB 2nqg Chain A

Receptor sequence
>2nqgA (length=322) Species: 10116 (Rattus norvegicus) [Search protein sequence]
NAIKYLGQDYENLRARCLQNGVLFQDDAFPPVSHSLGFKELGPNSSKTYG
IKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNETILH
RVVPYGQSFQEGYAGIFHFQLWQFGEWVDVVVDDLLPTKDGKLVFVHSAQ
GNEFWSALLEKAYAKVNGSYEALSGGCTSEAFEDFTGGVTEWYDLQKAPS
DLYQIILKALERGSLLGCSINISDIRDLEAITFKNLVRGHAYSVTDAKQV
TYQGQRVNLIRMRNPWGEVEWKGPWSDNSYEWNKVDPYEREQLRVKMEDG
EFWMSFRDFIREFTKLEICNLT
3D structure
PDB2nqg Development of Calpain-specific Inactivators by Screening of Positional Scanning Epoxide Libraries
ChainA
Resolution2.04 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 CA A V99 G101 D106 E185 V67 G69 D74 E153
BS02 CA A E302 D309 M329 D331 E333 E270 D277 M297 D299 E301
BS03 NQG A Q109 G113 C115 G208 S251 G271 H272 W298 Q77 G81 C83 G176 S219 G239 H240 W266 PDBbind-CN: -logKd/Ki=6.48,IC50=333nM
Gene Ontology
Molecular Function
GO:0004198 calcium-dependent cysteine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:2nqg, PDBe:2nqg, PDBj:2nqg
PDBsum2nqg
PubMed17218315
UniProtP97571|CAN1_RAT Calpain-1 catalytic subunit (Gene Name=Capn1)

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