Structure of PDB 2ary Chain A

Receptor sequence
>2aryA (length=322) Species: 9606 (Homo sapiens) [Search protein sequence]
NAIKYLGQDYEQLRVRCLQSGTLFRDEAFPPVPQSLGYKDLGPNSSKTYG
IKWKRPTELLSNPQFIVDGATRTDICQGALGDCWLLAAIASLTLNDTLLH
RVVPHGQSFQNGYAGIFHFQLWQFGEWVDVVVDDLLPIKDGKLVFVHSAE
GNEFWSALLEKAYAKVNGSYEALSGGSTSEGFEDFTGGVTEWYELRKAPS
DLYQIILKALERGSLLGCSIDISSVLDMEAITFKKLVKGHAYSVTGAKQV
NYRGQVVSLIRMRNPWGEVEWTGAWSDSSSEWNNVDPYERDQLRVKMEDG
EFWMSFRDFMREFTRLEICNLT
3D structure
PDB2ary The Crystal Structures of Human Calpains 1 and 9 Imply Diverse Mechanisms of Action and Auto-inhibition
ChainA
Resolution2.4 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 D100 G101 D106 E185 V67 D68 G69 D74 E153
BS02 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

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Molecular Function
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Biological Process
External links
PDB RCSB:2ary, PDBe:2ary, PDBj:2ary
PDBsum2ary
PubMed17157313
UniProtP07384|CAN1_HUMAN Calpain-1 catalytic subunit (Gene Name=CAPN1)

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