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Description
  • Background: Enzyme active sites can be connected to the exterior environment by one or more channels passing through the protein. Despite our current knowledge of enzyme structure and function, surprisingly little is known about how often channels are present or about any structural features such channels may have in common. Results: Here, we analyze the long channels (i.e. > 15 angstrom) leading to the active sites of 4,306 enzyme structures. We find that over 64% of enzymes contain two or more long channels, their typical length being 28 angstrom. We show that amino acid compositions of the channel significantly differ both to the composition of the active site, surface and interior of the protein. Conclusions: The majority of enzymes have buried active sites accessible via a network of access channels.
  • Background: Enzyme active sites can be connected to the exterior environment by one or more channels passing through the protein. Despite our current knowledge of enzyme structure and function, surprisingly little is known about how often channels are present or about any structural features such channels may have in common. Results: Here, we analyze the long channels (i.e. > 15 angstrom) leading to the active sites of 4,306 enzyme structures. We find that over 64% of enzymes contain two or more long channels, their typical length being 28 angstrom. We show that amino acid compositions of the channel significantly differ both to the composition of the active site, surface and interior of the protein. Conclusions: The majority of enzymes have buried active sites accessible via a network of access channels. (en)
Title
  • Anatomy of Enzyme Channels
  • Anatomy of Enzyme Channels (en)
skos:prefLabel
  • Anatomy of Enzyme Channels
  • Anatomy of Enzyme Channels (en)
skos:notation
  • RIV/00216224:14310/14:00077325!RIV15-MSM-14310___
http://linked.open...avai/riv/aktivita
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  • P(ED1.1.00/02.0068), P(ED2.1.00/03.0058), P(EE2.3.20.0058), P(GBP208/12/G016), P(GPP303/12/P019), S
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  • november
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  • 3253
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  • RIV/00216224:14310/14:00077325
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  • CATALYTIC SITE ATLAS; ACTIVE-SITE; ION CHANNELS; BIOMACROMOLECULAR CHANNELS; SUBSTRATE PREFERENCES; CYTOCHROMES P450; LIGAND-BINDING; ACCESS TUNNELS; PROTEIN; RESIDUES (en)
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  • GB - Spojené království Velké Británie a Severního Irska
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  • [B33E02A99604]
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  • BMC Bioinformatics
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  • 15
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  • Koča, Jaroslav
  • Otyepka, Michal
  • Berka, Karel
  • Sehnal, David
  • Svobodová Vařeková, Radka
  • Banáš, Pavel
  • Pravda, Lukáš
  • Roman A, Laskowski
http://linked.open...ain/vavai/riv/wos
  • 000345944500002
issn
  • 1471-2105
number of pages
http://bibframe.org/vocab/doi
  • 10.1186/s12859-014-0379-x
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  • 14310
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