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Ligands
Code Name Style Show Link
CA Calcium ion
FIN (1r)-1-{[(4'-methoxy-1,1'-biphenyl-4-yl)sulfonyl]amino}-2-methylpropylphosphonic acid
ZN Zinc ion
Non-standard Residues
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Code : 1ZVX   PDBj   RCSB PDB   PDBe
Header : HYDROLASE
Title : Crystal structure of the complex between MMP-8 and a phosphonate inhibitor (R-enantiomer)
Release Data : 2006-05-16
Compound :
mol_id molecule chains synonym
1 Neutrophil collagenase A Matrix metalloproteinase-8, MMP-8, PMNL collagenase, PMNL-CL
ec: 3.4.24.34
fragment: catalytic domain of neutrophil collagenase (Residues:80-242)
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli BL21  (taxid:511693)
gene: MMP8, CLG1
expression_system_strain: BL21
expression_system_plasmid: pSVB30
Authors : Pochetti, G., Gavuzzo, E., Campestre, C., Agamennone, M., Tortorella, P., Consalvi, V., Gallina, C., Hiller, O., Tschesche, H., Tucker, P.A., Mazza, F.
Keywords : stereoselective inhibition, phosphonic inhibitors, hydrolase, sulfonamide junction
Exp. method : X-RAY DIFFRACTION ( 1.87 Å )
Citation :

Structural insight into the stereoselective inhibition of MMP-8 by enantiomeric sulfonamide phosphonates.

Pochetti, G.,Gavuzzo, E.,Campestre, C.  et al.
(2006)  J.Med.Chem.  49 : 923 - 931

PubMed: 16451058
DOI: 10.1021/jm050787+

X-ray structure of human stromelysin catalytic domain complexed with nonpeptide inhibitors: implications for inhibitor selectivity

Pavlovsky, A.G.,Williams, M.G.,Ye, Q.Z.  et al.
(1999)  Protein Sci.  8 : 1455 - 1462

PubMed: 10422833

Two crystal structures of human neutrophil collagenase, one complexed with a primed- and the other with an unprimed-side inhibitor: implications for drug design

Gavuzzo, E.,Pochetti, G.,Mazza, F.  et al.
(2000)  J.Med.Chem.  43 : 3377 - 3385

PubMed: 10978185
DOI: 10.1021/jm9909589

X-ray structuresof human neutrophil collagenase complexed with peptide hydroxamate and peptide thiol inhibitors. Implications for substrate binding and rational drug design

Grams, F.,Reinemer, P.,Powers, J.C.  et al.
(1995)  Eur.J.Biochem.  228 : 830 - 841

PubMed: 7737183
DOI: 10.1111/j.1432-1033.1995.tb20329.x

Chain : A
UniProt : P22894 (MMP8_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I. 3.4.24.34 -
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