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PDBsum entry 4h49

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protein ligands metals Protein-protein interface(s) links
Hydrolase/hydrolase inhibitor PDB id
4h49
Jmol
Contents
Protein chains
159 a.a.
Ligands
PGO ×2
DMS
PEG ×4
L29 ×2
GOL
Metals
_ZN ×8
_CA ×12
Waters ×274
PDB id:
4h49
Name: Hydrolase/hydrolase inhibitor
Title: Crystal structure of the catalytic domain of mmp-12 in compl twin inhibitor.
Structure: Macrophage metalloelastase. Chain: a, b, c, d. Fragment: human mmp12 catalytic domain. Synonym: mme, macrophage elastase, me, hme, matrix metallop 12, mmp-12. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: hme, mmp12. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
2.16Å     R-factor:   0.170     R-free:   0.241
Authors: C.Antoni,E.A.Stura,L.Vera,E.Nuti,L.Carafa,E.Cassar-Lajeuness A.Rossello
Key ref: E.Nuti et al. Powerful twin carboxylic inhibitors for mmp homodimerisation.. To be published, .
Date:
17-Sep-12     Release date:   24-Apr-13    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P39900  (MMP12_HUMAN) -  Macrophage metalloelastase
Seq:
Struc:
470 a.a.
159 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.3.4.24.65  - Macrophage elastase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of soluble and insoluble elastin. Specific cleavages are also produced at 14-Ala-|-Leu-15 and 16-Tyr-|-Leu-17 in the B chain of insulin.
      Cofactor: Ca(2+); Zn(2+)
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular matrix   1 term 
  Biological process     wound healing   2 terms 
  Biochemical function     metallopeptidase activity     3 terms