Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3DF0

Calcium-dependent complex between m-calpain and calpastatin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000785	cellular_component	chromatin
A	0001666	biological_process	response to hypoxia
A	0001824	biological_process	blastocyst development
A	0004198	molecular_function	calcium-dependent cysteine-type endopeptidase activity
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005764	cellular_component	lysosome
A	0005783	cellular_component	endoplasmic reticulum
A	0005794	cellular_component	Golgi apparatus
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005925	cellular_component	focal adhesion
A	0006508	biological_process	proteolysis
A	0007520	biological_process	myoblast fusion
A	0007565	biological_process	female pregnancy
A	0008092	molecular_function	cytoskeletal protein binding
A	0008233	molecular_function	peptidase activity
A	0008234	molecular_function	cysteine-type peptidase activity
A	0009612	biological_process	response to mechanical stimulus
A	0009897	cellular_component	external side of plasma membrane
A	0010666	biological_process	positive regulation of cardiac muscle cell apoptotic process
A	0016020	cellular_component	membrane
A	0016540	biological_process	protein autoprocessing
A	0016787	molecular_function	hydrolase activity
A	0019899	molecular_function	enzyme binding
A	0030163	biological_process	protein catabolic process
A	0030425	cellular_component	dendrite
A	0031143	cellular_component	pseudopodium
A	0032675	biological_process	regulation of interleukin-6 production
A	0035458	biological_process	cellular response to interferon-beta
A	0042542	biological_process	response to hydrogen peroxide
A	0042995	cellular_component	cell projection
A	0043025	cellular_component	neuronal cell body
A	0044877	molecular_function	protein-containing complex binding
A	0045121	cellular_component	membrane raft
A	0046872	molecular_function	metal ion binding
A	0048266	biological_process	behavioral response to pain
A	0048488	biological_process	synaptic vesicle endocytosis
A	0051603	biological_process	proteolysis involved in protein catabolic process
A	0071222	biological_process	cellular response to lipopolysaccharide
A	0071230	biological_process	cellular response to amino acid stimulus
A	0097038	cellular_component	perinuclear endoplasmic reticulum
A	0098793	cellular_component	presynapse
A	0098794	cellular_component	postsynapse
A	0110158	cellular_component	calpain complex
A	0140249	biological_process	protein catabolic process at postsynapse
A	1901741	biological_process	positive regulation of myoblast fusion
A	2001247	biological_process	positive regulation of phosphatidylcholine biosynthetic process
B	0005509	molecular_function	calcium ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 715

Chain	Residue
A	ILE89
A	GLY90
A	GLY91
A	ASP96
A	GLU175

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 716

Chain	Residue
A	GLU323
A	GLU292
A	ASP299
A	GLN319
A	ASP321

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 717

Chain	Residue
A	ALA542
A	ASP545
A	ALA546
A	GLU547
A	GLU552

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 718

Chain	Residue
A	GLU547
A	ASP585
A	ASP587
A	SER589
A	LYS591
A	GLU596

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 719

Chain	Residue
A	ASP615
A	ASP617
A	SER619
A	THR621
A	GLU626

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 720

Chain	Residue
A	ASP570
A	ASP658
A	ASP660
A	ASN661

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 601

Chain	Residue
B	ALA111
B	ASP114
B	GLU116
B	GLU121

site_id	AC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CA B 602

Chain	Residue
B	GLU116
B	ASP154
B	ASP156
B	THR158
B	LYS160
B	LEU161
B	GLY162
B	GLU165

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA B 603

Chain	Residue
B	ASP184
B	ASP186
B	SER188
B	THR190
B	GLU195

site_id	BC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 604

Chain	Residue
B	ASP139
B	ASP227
B	ASP229
B	ASN230

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DSDTTGKLGfeEF

Chain	Residue	Details
B	ASP154-PHE166
B	ASP184-LEU196
A	ASP585-PHE597
A	ASP615-MET627

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	33
Details	Domain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	68
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	68
Details	Domain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	169
Details	Region: {"description":"Domain III"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	14
Details	Region: {"description":"Linker"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	170
Details	Region: {"description":"Domain IV"}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	3
Details	Active site: {"evidences":[{"source":"PubMed","id":"7635186","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	16
Details	Binding site: {}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	34
Details	Domain: {"description":"EF-hand 1; atypical","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	28
Details	Domain: {"description":"EF-hand 4","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	34
Details	Domain: {"description":"EF-hand 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19020622","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19020623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9228945","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DVI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DF0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19020622","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19020623","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9228945","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DVI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3BOW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DF0","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P04632","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1kfu

Chain	Residue	Details
A	ASN286
A	HIS262
A	GLN99
A	SER105

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1kfu

Chain	Residue	Details
A	ASN286
A	HIS262
A	GLN99
A	SER105
A	TRP288

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)