Structure of PDB 3df0 Chain A Binding Site BS06

Receptor Information
>3df0 Chain A (length=676) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
AIKYLNQDYETLRNECLEAGALFQDPSFPALPSSLGFKELGPYSSKTRGI
EWKRPTEICADPQFIIGGATRTDICQGALGDSWLLAAIASLTLNEEILAR
VVPLDQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEG
SEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELRKPPPN
LFKIIQKALEKGSLLGCSIDITSASEAVTYQKLVKGHAYSVTGAEEVESS
GSLQKLIRIRNPWGQVEWTGKWNDNCPSWNTVDPEVRANLTERQEDGEFW
MSFSDFLRHYSRLEICNLTPDTLTCDSYKKWKLTKMDGNWRRGSTAGGCR
NYPNTFWMNPQYLIKLEEEDEDDEDGERGCTFLVGLIQKHRRRQRKMGED
MHTIGFGIYEVPEELTGQTNIHLSKNFFLTTRARERSDTFINLREVLNRF
KLPPGEYVLVPSTFEPHKNGDFCIRVFSEKKADYQTVDDEIEANIEEIEA
NEEDIGDGFRRLFAQLAGEDAEISAFELQTILRRVLAKREDIKSDGFSIE
TCKIMVDMLDEDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSY
EMRKALEEAGFKLPCQLHQVIVARFADDELIIDFDNFVRCLVRLEILFKI
FKQLDPENTGTIQLDLISWLSFSVLG
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain3df0 Chain A Residue 720 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3df0 Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains.
Resolution2.95 Å
Binding residue
(original residue number in PDB)		D570 D658 D660 N661
Binding residue
(residue number reindexed from 1)		D545 D633 D635 N636
Annotation score4
Enzymatic activity
Catalytic site (original residue number in PDB) Q99 S105 H262 N286 W288
Catalytic site (residue number reindexed from 1) Q76 S82 H237 N261 W263
Enzyme Commision number 3.4.22.53: calpain-2.
Gene Ontology
Molecular Function
GO:0004198 calcium-dependent cysteine-type endopeptidase activity
GO:0005509 calcium ion binding
GO:0005515 protein binding
GO:0008092 cytoskeletal protein binding
GO:0008233 peptidase activity
GO:0008234 cysteine-type peptidase activity
GO:0019899 enzyme binding
GO:0044877 protein-containing complex binding
GO:0046872 metal ion binding
Biological Process
GO:0001666 response to hypoxia
GO:0001824 blastocyst development
GO:0006508 proteolysis
GO:0007520 myoblast fusion
GO:0007565 female pregnancy
GO:0009612 response to mechanical stimulus
GO:0010666 positive regulation of cardiac muscle cell apoptotic process
GO:0016540 protein autoprocessing
GO:0030163 protein catabolic process
GO:0032675 regulation of interleukin-6 production
GO:0035458 cellular response to interferon-beta
GO:0042542 response to hydrogen peroxide
GO:0048266 behavioral response to pain
GO:0048488 synaptic vesicle endocytosis
GO:0051603 proteolysis involved in protein catabolic process
GO:0071222 cellular response to lipopolysaccharide
GO:0071230 cellular response to amino acid stimulus
GO:0140249 protein catabolic process at postsynapse
GO:1901741 positive regulation of myoblast fusion
GO:2001247 positive regulation of phosphatidylcholine biosynthetic process
Cellular Component
GO:0000785 chromatin
GO:0005634 nucleus
GO:0005737 cytoplasm
GO:0005764 lysosome
GO:0005783 endoplasmic reticulum
GO:0005794 Golgi apparatus
GO:0005829 cytosol
GO:0005886 plasma membrane
GO:0005925 focal adhesion
GO:0009897 external side of plasma membrane
GO:0030425 dendrite
GO:0031143 pseudopodium
GO:0042995 cell projection
GO:0043025 neuronal cell body
GO:0045121 membrane raft
GO:0097038 perinuclear endoplasmic reticulum
GO:0098793 presynapse
GO:0098794 postsynapse
GO:0110158 calpain complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3df0, PDBe:3df0, PDBj:3df0
PDBsum3df0
PubMed19020622
UniProtQ07009|CAN2_RAT Calpain-2 catalytic subunit (Gene Name=Capn2)

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