Structure of PDB 3df0 Chain A
Receptor sequence
>3df0A (length=676) Species:
10116
(Rattus norvegicus) [
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AIKYLNQDYETLRNECLEAGALFQDPSFPALPSSLGFKELGPYSSKTRGI
EWKRPTEICADPQFIIGGATRTDICQGALGDSWLLAAIASLTLNEEILAR
VVPLDQSFQENYAGIFHFQFWQYGEWVEVVVDDRLPTKDGELLFVHSAEG
SEFWSALLEKAYAKINGCYEALSGGATTEGFEDFTGGIAEWYELRKPPPN
LFKIIQKALEKGSLLGCSIDITSASEAVTYQKLVKGHAYSVTGAEEVESS
GSLQKLIRIRNPWGQVEWTGKWNDNCPSWNTVDPEVRANLTERQEDGEFW
MSFSDFLRHYSRLEICNLTPDTLTCDSYKKWKLTKMDGNWRRGSTAGGCR
NYPNTFWMNPQYLIKLEEEDEDDEDGERGCTFLVGLIQKHRRRQRKMGED
MHTIGFGIYEVPEELTGQTNIHLSKNFFLTTRARERSDTFINLREVLNRF
KLPPGEYVLVPSTFEPHKNGDFCIRVFSEKKADYQTVDDEIEANIEEIEA
NEEDIGDGFRRLFAQLAGEDAEISAFELQTILRRVLAKREDIKSDGFSIE
TCKIMVDMLDEDGSGKLGLKEFYILWTKIQKYQKIYREIDVDRSGTMNSY
EMRKALEEAGFKLPCQLHQVIVARFADDELIIDFDNFVRCLVRLEILFKI
FKQLDPENTGTIQLDLISWLSFSVLG
3D structure
PDB
3df0
Concerted multi-pronged attack by calpastatin to occlude the catalytic cleft of heterodimeric calpains.
Chain
A
Resolution
2.95 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 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.
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 G90 G91 D96 E175
I66 G67 G68 D73 E152
BS02
CA
A
E292 D299 Q319 D321 E323
E267 D274 Q294 D296 E298
BS03
CA
A
A542 D545 A546 E547 I548 E552
A517 D520 A521 E522 I523 E527
BS04
CA
A
E547 D585 D587 S589 K591 E596
E522 D560 D562 S564 K566 E571
BS05
CA
A
D615 D617 S619 T621 E626
D590 D592 S594 T596 E601
BS06
CA
A
D570 D658 D660 N661
D545 D633 D635 N636
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:3df0
,
PDBe:3df0
,
PDBj:3df0
PDBsum
3df0
PubMed
19020622
UniProt
Q07009
|CAN2_RAT Calpain-2 catalytic subunit (Gene Name=Capn2)
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