1a85 Summary

pdbe.org/1a85
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MMP8 WITH MALONIC AND ASPARAGINE BASED INHIBITOR

The structure was published by Brandstetter, H., Engh, R.A., Von Roedern, E.G., et al., Huber, R., Bode, W., and Grams, F., in 1998 in a paper entitled "Structure of malonic acid-based inhibitors bound to human neutrophil collagenase. A new binding mode explains apparently anomalous data." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 1998.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of MMP-8. This molecule has the UniProt identifier P22894 (MMP8_HUMAN)search. The sample contained 158 residues which is < 90% of the natural sequence. Out of 158 residues 157 were observed and are deposited in the PDB.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A MMP-8 P22894 (105-262) (MMP8_HUMAN)search Homo sapienssearch < 90% 158 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P22894 (105 - 262) MMP-8 Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Matrix metalloproteases, catalytic domainsearch Collagenase (Catalytic Domain)search Matrixinsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P22894) zinc ion bindingsearch metalloendopeptidase activitysearch metallopeptidase activitysearch proteolysissearch extracellular matrixsearch

Chain InterPro annotation
A Peptidase M10, metallopeptidasesearch Peptidase, metallopeptidasesearch Peptidase M10Asearch Metallopeptidase, catalytic domainsearch