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PDBsum entry 4i03

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protein ligands metals links
Hydrolase/hydrolase inhibitor PDB id
4i03
Jmol
Contents
Protein chain
159 a.a.
Ligands
L88
GOL ×3
PGO ×2
DMS ×2
EDO ×4
PEG
Metals
_ZN ×2
_CA ×3
Waters ×171
PDB id:
4i03
Name: Hydrolase/hydrolase inhibitor
Title: Human mmp12 in complex with a peg-linked bifunctional l-glut motif inhibitor
Structure: Macrophage metalloelastase. Chain: a. Fragment: catalytic domain (unp residues 106-263). Synonym: mme, macrophage elastase, me, hme, matrix metallop 12, mmp-12. Engineered: yes. Mutation: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Strain: escherichia coli. Gene: hme, mmp12. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.70Å     R-factor:   0.146     R-free:   0.194
Authors: E.A.Stura,L.Vera,L.Devel,E.Cassar-Lajeunesse,V.Dive
Key ref: C.Antoni et al. (2013). Crystallization of bi-functional ligand protein complexes. J Struct Biol, 182, 246-254. PubMed id: 23567804 DOI: 10.1016/j.jsb.2013.03.015
Date:
16-Nov-12     Release date:   24-Apr-13    
PROCHECK
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 Headers
 References

Protein chain
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 3 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  

 

 
DOI no: 10.1016/j.jsb.2013.03.015 J Struct Biol 182:246-254 (2013)
PubMed id: 23567804  
 
 
Crystallization of bi-functional ligand protein complexes.
C.Antoni, L.Vera, L.Devel, M.P.Catalani, B.Czarny, E.Cassar-Lajeunesse, E.Nuti, A.Rossello, V.Dive, E.A.Stura.
 
  ABSTRACT  
 
No abstract given.