1FBM
ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN IN COMPLEX WITH ALL-TRANS RETINOL
Summary for 1FBM
Entry DOI | 10.2210/pdb1fbm/pdb |
Related | 1VDF |
Descriptor | PROTEIN (CARTILAGE OLIGOMERIC MATRIX PROTEIN), RETINOL (3 entities in total) |
Functional Keywords | extracellular matrix protein, assembly domain, cartilage, oligomeric matrix protein, glycoprotein, retinol-complex, cell adhesion |
Biological source | Rattus norvegicus (Norway rat) |
Cellular location | Secreted, extracellular space, extracellular matrix : P35444 |
Total number of polymer chains | 5 |
Total formula weight | 26782.10 |
Authors | Guo, Y.,Bozic, D.,Malashkevich, V.N.,Kammerer, R.A.,Schulthess, T. (deposition date: 2000-07-16, release date: 2000-08-02, Last modification date: 2024-10-09) |
Primary citation | Guo, Y.,Bozic, D.,Malashkevich, V.N.,Kammerer, R.A.,Schulthess, T. All-trans retinol, vitamin D and other hydrophobic compounds bind in the axial pore of the five-stranded coiled-coil domain of cartilage oligomeric matrix protein. EMBO J., 17:5265-5272, 1998 Cited by PubMed: 9736606DOI: 10.1093/emboj/17.18.5265 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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