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CL0008 : Chain A, Crystal Structure Of Calcium-Bound Protease Core Of Calpain Ii Reveals The Basis For Intrinsic Inactivation

[ CaMP Format ]

* Basic Information

OrganismRattus norvegicus (Norway rat)
Protein NamesCalpain-2 catalytic subunit;; Calpain-2 large subunit; Calcium-activated neutral proteinase 2; CANP 2; Calpain M-type; M-calpain; Millimolar-calpain
Gene NamesCapn2
Gene LocusNot available
GO FunctionNot available
Entrez Protein Entrez Nucleotide Entrez Gene UniProt OMIM HGNC HPRD KEGG
1MDW_A N/A N/A Q07009 N/A N/A N/A rno:29154

* Information From OMIM

Not Available.

* Structure Information

1. Primary Information

Length: 328 aa

Average Mass: 36.774 kDa

Monoisotopic Mass: 36.751 kDa

2. Domain Information

Annotated Domains: interpro / pfam / smart / prosite

Computationally Assigned Domains (Pfam+HMMER):

domain namebeginendscoree-value
Peptidase_C2 1. 27326802.72.3e-238

3. Sequence Information

Fasta Sequence: CL0008.fasta

Amino Acid Sequence and Secondary Structures (PsiPred):

4. 3D Information

Known Structures in PDB: 1DF0 (X-ray; 260 A; A=1-700), 1MDW (X-ray; 195 A; A/B=19-346), 1QXP (X-ray; 280 A; A/B=-), 1U5I (X-ray; 286 A; A=1-700)

* References

[PubMed ID: 10601010] Hosfield CM, Elce JS, Davies PL, Jia Z, Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation. EMBO J. 1999 Dec 15;18(24):6880-9.

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