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PDBsum entry 1os2
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Contents |
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* Residue conservation analysis
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PDB id:
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Hydrolase
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Title:
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Ternary enzyme-product-inhibitor complexes of human mmp12
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Structure:
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Macrophage metalloelastase. Chain: a, b, c, d, e, f. Synonym: hme, matrix metalloproteinase-12, mmp-12, macrophage elastase, me. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: mmp12 or hme. Expressed in: escherichia coli. Expression_system_taxid: 562
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Resolution:
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2.15Å
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R-factor:
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0.215
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R-free:
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0.271
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Authors:
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I.Bertini,V.Calderone,M.Fragai,C.Luchinat,S.Mangani,B.Terni
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Key ref:
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I.Bertini
et al.
(2003).
X-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinases.
Angew Chem Int Ed Engl,
42,
2673-2676.
PubMed id:
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Date:
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18-Mar-03
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Release date:
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05-Aug-03
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PROCHECK
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Headers
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References
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P39900
(MMP12_HUMAN) -
Macrophage metalloelastase from Homo sapiens
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Seq:
Struc:
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470 a.a.
165 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 3 residue positions (black
crosses)
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Enzyme class:
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E.C.3.4.24.65
- macrophage elastase.
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Reaction:
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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.
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Cofactor:
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Ca(2+); Zn(2+)
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Angew Chem Int Ed Engl
42:2673-2676
(2003)
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PubMed id:
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X-ray structures of binary and ternary enzyme-product-inhibitor complexes of matrix metalloproteinases.
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I.Bertini,
V.Calderone,
M.Fragai,
C.Luchinat,
S.Mangani,
B.Terni.
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ABSTRACT
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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I.Bertini,
M.Fragai,
C.Luchinat,
M.Melikian,
and
C.Venturi
(2009).
Characterisation of the MMP-12-elastin adduct.
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Chemistry,
15,
7842-7845.
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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).
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J Biol Chem,
284,
12821-12828.
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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.
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J Biol Chem,
283,
21779-21788.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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Links
