- EMDB-49572: Structure of the HERV-K (HML-2) spike complex -
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基本情報
登録情報
データベース: EMDB / ID: EMD-49572
タイトル
Structure of the HERV-K (HML-2) spike complex
マップデータ
Main map - unfiltered
試料
複合体: The HERV-K spike complex
タンパク質・ペプチド: Endogenous retrovirus group K member 7 Pol protein
タンパク質・ペプチド: Surface protein
リガンド: 2-acetamido-2-deoxy-beta-D-glucopyranose
リガンド: water
キーワード
HERV-K Endogenous retrovirus K Spike protein Viral glycoprotein / VIRAL PROTEIN / HML-2
機能・相同性
機能・相同性情報
ribonuclease H / DNA synthesis involved in DNA repair / RNA-directed DNA polymerase activity / DNA integration / RNA-directed DNA polymerase / DNA-templated DNA replication / RNA stem-loop binding / RNA-DNA hybrid ribonuclease activity / DNA recombination / structural molecule activity ...ribonuclease H / DNA synthesis involved in DNA repair / RNA-directed DNA polymerase activity / DNA integration / RNA-directed DNA polymerase / DNA-templated DNA replication / RNA stem-loop binding / RNA-DNA hybrid ribonuclease activity / DNA recombination / structural molecule activity / DNA binding / zinc ion binding / plasma membrane 類似検索 - 分子機能
Retro-transcribing virus envelope glycoprotein / : / Retro-transcribing viruses envelope glycoprotein / Rec (regulator of expression encoded by corf) of HERV-K-113 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Reverse transcriptase thumb / Reverse transcriptase thumb domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. ...Retro-transcribing virus envelope glycoprotein / : / Retro-transcribing viruses envelope glycoprotein / Rec (regulator of expression encoded by corf) of HERV-K-113 / Retroviral envelope protein / Retroviral envelope protein GP41-like / Reverse transcriptase thumb / Reverse transcriptase thumb domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. / Integrase-like, N-terminal / Integrase DNA binding domain / Integrase, C-terminal domain superfamily, retroviral / Integrase, N-terminal zinc-binding domain / Integrase, C-terminal, retroviral / Integrase DNA binding domain profile. / RNase H / Integrase core domain / Integrase, catalytic core / Integrase catalytic domain profile. / RNase H type-1 domain profile. / Ribonuclease H domain / Reverse transcriptase domain / Reverse transcriptase (RNA-dependent DNA polymerase) / Reverse transcriptase (RT) catalytic domain profile. / Ribonuclease H superfamily / Ribonuclease H-like superfamily / Reverse transcriptase/Diguanylate cyclase domain / DNA/RNA polymerase superfamily 類似検索 - ドメイン・相同性
Endogenous retrovirus group K member 25 Env polyprotein / Endogenous retrovirus group K member 7 Pol protein 類似検索 - 構成要素
ジャーナル: Acta Crystallogr D Struct Biol / 年: 2019 タイトル: Macromolecular structure determination using X-rays, neutrons and electrons: recent developments in Phenix. 著者: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / ...著者: Dorothee Liebschner / Pavel V Afonine / Matthew L Baker / Gábor Bunkóczi / Vincent B Chen / Tristan I Croll / Bradley Hintze / Li Wei Hung / Swati Jain / Airlie J McCoy / Nigel W Moriarty / Robert D Oeffner / Billy K Poon / Michael G Prisant / Randy J Read / Jane S Richardson / David C Richardson / Massimo D Sammito / Oleg V Sobolev / Duncan H Stockwell / Thomas C Terwilliger / Alexandre G Urzhumtsev / Lizbeth L Videau / Christopher J Williams / Paul D Adams / 要旨: Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological ...Diffraction (X-ray, neutron and electron) and electron cryo-microscopy are powerful methods to determine three-dimensional macromolecular structures, which are required to understand biological processes and to develop new therapeutics against diseases. The overall structure-solution workflow is similar for these techniques, but nuances exist because the properties of the reduced experimental data are different. Software tools for structure determination should therefore be tailored for each method. Phenix is a comprehensive software package for macromolecular structure determination that handles data from any of these techniques. Tasks performed with Phenix include data-quality assessment, map improvement, model building, the validation/rebuilding/refinement cycle and deposition. Each tool caters to the type of experimental data. The design of Phenix emphasizes the automation of procedures, where possible, to minimize repetitive and time-consuming manual tasks, while default parameters are chosen to encourage best practice. A graphical user interface provides access to many command-line features of Phenix and streamlines the transition between programs, project tracking and re-running of previous tasks.