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6ELY

Crystal Structure of Mistletoe Lectin I (ML-I) from Viscum album in Complex with 4-N-Furfurylcytosine at 2.84 A Resolution

Summary for 6ELY
Entry DOI10.2210/pdb6ely/pdb
DescriptorMistletoe Lectin I, 4-N-Furfurylcytosine, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (11 entities in total)
Functional Keywordsribosome-inactivating protein, mistletoe lectin, viscum album l., 4-n-furfurylcytosine, hydrolase
Biological sourceViscum album
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Total number of polymer chains2
Total formula weight59940.65
Authors
Ahmad, M.S.,Rasheed, S.,Falke, S.,Khaliq, B.,Perbandt, M.,Choudhary, M.I.,Markiewicz, W.T.,Barciszewski, J.,Betzel, C. (deposition date: 2017-09-30, release date: 2018-05-02, Last modification date: 2024-01-17)
Primary citationAhmad, M.S.,Rasheed, S.,Falke, S.,Khaliq, B.,Perbandt, M.,Choudhary, M.I.,Markiewicz, W.T.,Barciszewski, J.,Betzel, C.
Crystal Structure of Mistletoe Lectin I (ML-I) from Viscum album in Complex with 4-N-Furfurylcytosine at 2.85 angstrom Resolution.
Med Chem, 14:754-763, 2018
Cited by
PubMed Abstract: Viscum album (the European mistletoe) is a semi-parasitic plant, which is of high medical interest. It is widely found in Europe, Asia, and North America. It contains at least three distinct lectins (i.e. ML-I, II, and III), varying in molecular mass and specificity. Among them, ML-I is in focus of medical research for various activities, including anti-cancer activities. To understand the molecular basis for such medical applications, a few studies have already addressed the structural and functional analysis of ML-I in complex with ligands. In continuation of these efforts, we are reporting the crystal structure of ML from Viscum album in complex with the nucleic acid oxidation product 4-N-furfurylcytosine (FC) refined to 2.85 Å resolution. FC is known to be involved in different metabolic pathways related to oxidative stress and DNA modification.
PubMed: 29792147
DOI: 10.2174/1573406414666180524095946
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.84 Å)
Structure validation

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