PDBsum entry 2oxw

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Hydrolase PDB id
Protein chain
158 a.a. *
_CA ×3
_ZN ×2
Waters ×199
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Human mmp-12 complexed with the peptide iag
Structure: Macrophage metalloelastase. Chain: a. Fragment: catalytic domain. Synonym: hme, matrix metalloproteinase-12, mmp-12, macrophage elastase, me. Engineered: yes. Mutation: yes. Ile-ala-gly peptide. Chain: x.
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: mmp12, hme. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Synthetic: yes
1.15Å     R-factor:   0.199     R-free:   0.223
Authors: V.Calderone,I.Bertini,M.Fragai,C.Luchinat,M.Maletta,K.J.Yeo
Key ref: I.Bertini et al. (2006). Snapshots of the reaction mechanism of matrix metalloproteinases. Angew Chem Int Ed Engl, 45, 7952-7955. PubMed id: 17096442
21-Feb-07     Release date:   06-Mar-07    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P39900  (MMP12_HUMAN) -  Macrophage metalloelastase
470 a.a.
158 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - 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  


Angew Chem Int Ed Engl 45:7952-7955 (2006)
PubMed id: 17096442  
Snapshots of the reaction mechanism of matrix metalloproteinases.
I.Bertini, V.Calderone, M.Fragai, C.Luchinat, M.Maletta, K.J.Yeo.
No abstract given.


Literature references that cite this PDB file's key reference

  PubMed id Reference
19609998 I.Bertini, M.Fragai, C.Luchinat, M.Melikian, and C.Venturi (2009).
Characterisation of the MMP-12-elastin adduct.
  Chemistry, 15, 7842-7845.  
19282283 I.Bertini, M.Fragai, C.Luchinat, M.Melikian, E.Mylonas, N.Sarti, and D.I.Svergun (2009).
Interdomain Flexibility in Full-length Matrix Metalloproteinase-1 (MMP-1).
  J Biol Chem, 284, 12821-12828.  
19707688 M.Rouffet, C.Denhez, E.Bourguet, F.Bohr, and D.Guillaume (2009).
In silico study of MMP inhibition.
  Org Biomol Chem, 7, 3817-3825.  
19131516 P.J.Baker, K.L.Britton, M.Fisher, J.Esclapez, C.Pire, M.J.Bonete, J.Ferrer, and D.W.Rice (2009).
Active site dynamics in the zinc-dependent medium chain alcohol dehydrogenase superfamily.
  Proc Natl Acad Sci U S A, 106, 779-784.
PDB codes: 2vwg 2vwh 2vwp 2vwq
18604568 C.Andreini, I.Bertini, G.Cavallaro, G.L.Holliday, and J.M.Thornton (2008).
Metal ions in biological catalysis: from enzyme databases to general principles.
  J Biol Inorg Chem, 13, 1205-1218.  
17963710 I.Sagi, and M.E.Milla (2008).
Application of structural dynamic approaches provide novel insights into the enzymatic mechanism of the tumor necrosis factor-alpha-converting enzyme.
  Anal Biochem, 372, 1.  
18539597 R.Bhaskaran, M.O.Palmier, J.L.Lauer-Fields, G.B.Fields, and S.R.Van Doren (2008).
MMP-12 catalytic domain recognizes triple helical peptide models of collagen V with exosites and high activity.
  J Biol Chem, 283, 21779-21788.  
17710450 L.A.Alcaraz, L.Banci, I.Bertini, F.Cantini, A.Donaire, and L.Gonnelli (2007).
Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors.
  J Biol Inorg Chem, 12, 1197-1206.
PDB codes: 2jnp 2jt5 2jt6
17997411 R.Bhaskaran, M.O.Palmier, N.A.Bagegni, X.Liang, and S.R.Van Doren (2007).
Solution structure of inhibitor-free human metalloelastase (MMP-12) indicates an internal conformational adjustment.
  J Mol Biol, 374, 1333-1344.
PDB code: 2poj
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