Structure of PDB 3bow Chain A

Receptor sequence
>3bowA (length=680) Species: 10116 (Rattus norvegicus) [Search protein sequence]
RAIKYLNQDYETLRNECLEAGALFQDPSFPALPSSLGFKELGPYSSKTRG
IEWKRPTEICADPQFIIGGATRTDICQGALGDSWLLAAIASLTLNEEILA
RVVPLDQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAE
GSEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELRKPPP
NLFKIIQKALEKGSLLGCSIDITSAADSEAVTYQKLVKGHAYSVTGAEEV
ESSGSLQKLIRIRNPWGQVEWTGKWNDNCPSWNTVDPEVRANLTERQEDG
EFWMSFSDFLRHYSRLEICNLTPDTLTCDSYKKWKLTKMDGNWRRGSTAG
GCRNYPNTFWMNPQYLIKLEEEDEDDEDGERGCTFLVGLIQKHRRRQRKM
GEDMHTIGFGIYEVPEELTGQTNIHLSKNFFLTTRARERSDTFINLREVL
NRFKLPPGEYVLVPSTFEPHKNGDFCIRVFSEKKADYVDDEIEANIEEIE
ANEEDIGDGFRRLFAQLAGEDAEISAFELQTILRRVLAKREDIKSDGFSI
ETCKIMVDMLDEDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNS
YEMRKALEEAGFKLPCQLHQVIVARFADDELIIDFDNFVRCLVRLEILFK
IFKQLDPENTGTIQLDLISWLSFSVLGKLA
3D structure
PDB3bow Calcium-bound structure of calpain and its mechanism of inhibition by calpastatin.
ChainA
Resolution2.4 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) Q99 S105 H262 N286 W288
Catalytic site (residue number reindexed from 1) Q77 S83 H240 N264 W266
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 CA A I89 G91 D96 E175 I67 G69 D74 E153
BS02 CA A E292 D299 Q319 D321 E323 E270 D277 Q297 D299 E301
BS03 CA A A542 D545 E547 E552 A518 D521 E523 E528
BS04 CA A D585 D587 S589 K591 E596 D561 D563 S565 K567 E572
BS05 CA A D615 D617 S619 T621 E626 D591 D593 S595 T597 E602
BS06 CA A D658 D660 N661 D634 D636 N637
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3bow, PDBe:3bow, PDBj:3bow
PDBsum3bow
PubMed19020623
UniProtQ07009|CAN2_RAT Calpain-2 catalytic subunit (Gene Name=Capn2)

[Back to BioLiP]