1DF0
Crystal structure of M-Calpain
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 | 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 PROSITE/UniProt
site_id | PS00018 |
Number of Residues | 13 |
Details | EF_HAND_1 EF-hand calcium-binding domain. DEDGSGKLGlkEF |
Chain | Residue | Details |
A | ASP585-PHE597 | |
A | ASP615-MET627 | |
B | ASP68-PHE80 | |
B | ASP98-LEU110 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 17 |
Details | Propeptide: {"description":"Anchors to the small subunit","featureId":"PRO_0000026493","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
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_FI3 |
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_FI4 |
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_FI5 |
Number of Residues | 3 |
Details | Active site: {"evidences":[{"source":"PubMed","id":"7635186","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 13 |
Details | Binding site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P17655","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 34 |
Details | Domain: {"description":"EF-hand 1; atypical","evidences":[{"evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 28 |
Details | Domain: {"description":"EF-hand 4","evidences":[{"evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
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_FI12 |
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_FI13 |
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_FI14 |
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 |