Structure of PDB 2nqa Chain A

Receptor sequence
>2nqaA (length=310) Species: 9606 (Homo sapiens) [Search protein sequence]
NALKYLGQDFKTLRQQCLDSGVLFKDPEFPACPSALGYTQGIIWKRPTEL
CPSPQFIVGGATRTDICQGGLGDCWLLAAIASLTLNEELLYRVVPRDQDF
QENYAGIFHFQFWQYGEWVEVVIDDRLPTKNGQLLFLHSEQGNEFWSALL
EKAYAKLNGCYEALAGGSTVEGFEDFTGGISEFYDLKKPPANLYQIIRKA
LCAGSLLGCSIDVYSAAEAEAITSQKLVKSHAYSVTGVEEVNFQGHPEKL
IRLRNPWGEEWSGAWSDDAPEWNHIDPRRKEELDKKVEDGEFWMSLSDFV
RQFSRLEICN
3D structure
PDB2nqa Structure of Human Calpain 8
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q99 C105 H262 N286 W288
Catalytic site (residue number reindexed from 1) Q68 C74 H231 N255 W257
Enzyme Commision number 3.4.22.53: calpain-2.
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 G103 C105 G197 E251 S261 H262 G72 C74 G166 E220 S230 H231
BS02 CA A E292 D299 V319 D321 E323 E260 D267 V287 D289 E291
BS03 CA A V89 G91 D96 E175 V58 G60 D65 E144
BS04 CA A E292 E320 E260 E288
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:2nqa, PDBe:2nqa, PDBj:2nqa
PDBsum2nqa
PubMed
UniProtP17655|CAN2_HUMAN Calpain-2 catalytic subunit (Gene Name=CAPN2)

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