1L6J
Crystal structure of human matrix metalloproteinase MMP9 (gelatinase B).
Summary for 1L6J
| Entry DOI | 10.2210/pdb1l6j/pdb |
| Descriptor | Matrix metalloproteinase-9, ZINC ION, CALCIUM ION, ... (4 entities in total) |
| Functional Keywords | twisted beta sheet flanked by helices, hydrolase |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted, extracellular space, extracellular matrix (Probable): P14780 |
| Total number of polymer chains | 1 |
| Total formula weight | 47595.51 |
| Authors | Elkins, P.A.,Ho, Y.S.,Smith, W.W.,Janson, C.A.,D'Alessio, K.J.,McQueney, M.S.,Cummings, M.D.,Romanic, A.M. (deposition date: 2002-03-11, release date: 2002-07-03, Last modification date: 2024-10-16) |
| Primary citation | Elkins, P.A.,Ho, Y.S.,Smith, W.W.,Janson, C.A.,D'Alessio, K.J.,McQueney, M.S.,Cummings, M.D.,Romanic, A.M. Structure of the C-terminally truncated human ProMMP9, a gelatin-binding matrix metalloproteinase. Acta Crystallogr.,Sect.D, 58:1182-1192, 2002 Cited by PubMed Abstract: The X-ray crystal structure of the proform of human matrix metalloproteinase MMP9 has been solved to 2.5 A resolution. The construct includes the prodomain, the catalytic domain and three FnII (fibronectin type II) domains. The prodomain is inserted into the active-site cleft, blocking access to the catalytic zinc. Comparison with the crystal structure of the most closely related MMP, MMP2, indicates that the conformations of residues in the active-site cleft and in the cysteine-switch peptide of the prodomain are highly conserved and that design of MMP9-specific inhibitors will be challenging. In common with MMP2, the MMP9 S1' inhibitor-binding pocket is large compared with that of other MMPs. One small point of difference in the S1' binding pockets of MMP9 and MMP2 may provide an opportunity to explore the design of specific inhibitors. The side chain of Arg424 in MMP9 is angled slightly away from the S1' pocket when compared with the corresponding residue in MMP2, Thr424. The secondary structure of the FnII domains is conserved between the two closely related MMPs, although the second FnII domain makes no contact with the catalytic domain in MMP9, while the same domain in MMP2 has a substantial area of interaction with the catalytic domain. PubMed: 12077439DOI: 10.1107/S0907444902007849 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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