1FBM

ASSEMBLY DOMAIN OF CARTILAGE OLIGOMERIC MATRIX PROTEIN IN COMPLEX WITH ALL-TRANS RETINOL

Summary for 1FBM

Related1VDF
DescriptorPROTEIN (CARTILAGE OLIGOMERIC MATRIX PROTEIN), RETINOL (3 entities in total)
Functional Keywordsextracellular matrix protein, assembly domain, cartilage, oligomeric matrix protein, glycoprotein, retinol-complex, cell adhesion
Biological sourceRattus norvegicus (Norway rat)
Cellular locationSecreted, extracellular space, extracellular matrix  P35444
Total number of polymer chains5
Total molecular weight26782.1
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: 2018-02-28)
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
PubMed: 9736606 (PDB entries with the same primary citation)
DOI: 10.1093/emboj/17.18.5265
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.7 Å)
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Structure validation

ClashscoreRamachandran outliersSidechain outliers232.3%10.2%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution