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PDBsum entry 2nqa

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protein ligands metals Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
2nqa
Jmol
Contents
Protein chain
310 a.a. *
Ligands
ACE-LEU-LEU-AR7 ×2
Metals
_CA ×5
Waters ×308
* Residue conservation analysis
PDB id:
2nqa
Name: Hydrolase/hydrolase inhibitor
Title: Catalytic domain of human calpain 8
Structure: Calpain 8. Chain: a, b. Fragment: residues 23-346. Engineered: yes. Leupeptin inhibitor. Chain: d, e. Fragment: leupeptin inhibitor. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: loc388743. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes. Other_details: commercially available from sigma l2884
Biol. unit: Tetramer (from PQS)
Resolution:
2.20Å     R-factor:   0.205     R-free:   0.268
Authors: T.L.Davis,R.Paramanathan,C.Butler-Cole,P.J.Finerty Jr.,J.Wei M.Sundstrom,C.H.Arrowsmith,A.M.Edwards,A.Bochkarev,S.Dhe-Pa Structural Genomics Consortium (Sgc)
Key ref: T.L.Davis et al. Structure of human calpain 8. To be published, .
Date:
30-Oct-06     Release date:   14-Nov-06    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P17655  (CAN2_HUMAN) -  Calpain-2 catalytic subunit
Seq:
Struc:
 
Seq:
Struc:
700 a.a.
310 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 83 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.4.22.53  - Calpain-2.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Cofactor: Ca(2+)
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     intracellular   1 term 
  Biological process     digestion   2 terms 
  Biochemical function     calcium ion binding     2 terms