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dimer
the enzyme includes two subunits: an alpha subunit (GGTalpha), the catalytic subunit, that is shared with farnesyltransferase, EC 2.5.1.58, and a distinct beta subunit (GGTbeta), which is responsible for substrate binding
dimer
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the enzyme includes two subunits: an alpha subunit (GGTalpha), the catalytic subunit, that is shared with farnesyltransferase, EC 2.5.1.58, and a distinct beta subunit (GGTbeta), which is responsible for substrate binding
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heterodimer
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1 * 48000 + 1 * 40000
heterodimer
1 * 37000 + 1 * 45000
heterodimer
alphabeta, 1 * 48000, alpha-subunit
heterodimer
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1 * 43000 + 1 * 48000
heterodimer
alphabeta, 1 * 48000, alpha-subunit
heterodimer
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alpha,beta, 1 * 48000 + 1 * 43000
heterodimer
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alpha,beta, 1 * 34000 + 1 * 42000
additional information
both alpha and beta subunits are composed primarily of alpha helices. The beta subunits of GGTI consist of 13 alpha helices, and 12 of them are folded into an alpha-alpha barrel. The helices of the alpha subunit are arranged in a crescent-shaped superhelix that wraps around the alpha-alpha barrel of beta subunit. This arrangement creates a deep, funnel-shaped cavity in the center of the barrel, and the active sites of GGTI are located within this cavity
additional information
both alpha and beta subunits are composed primarily of alpha helices. The beta subunits of GGTI consist of 13 alpha helices, and 12 of them are folded into an alpha-alpha barrel. The helices of the alpha subunit are arranged in a crescent-shaped superhelix that wraps around the alpha-alpha barrel of beta subunit. This arrangement creates a deep, funnel-shaped cavity in the center of the barrel, and the active sites of GGTI are located within this cavity
additional information
the alpha subunit is primarily composed of alpha helices that are arranged into different shapes. The alpha subunit is a crescent-shaped super helix. The N-terminal domain is disordered and proline-rich, and has no direct influence on the catalytic activity
additional information
the alpha subunit is primarily composed of alpha helices that are arranged into different shapes. The alpha subunit is a crescent-shaped super helix. The N-terminal domain is disordered and proline-rich, and has no direct influence on the catalytic activity
additional information
the beta subunit is primarily composed of alpha helices that are arranged into different shapes. The beta subunit is an alpha-alpha barrel. The beta subunit of GGTase-I consists of 13 alpha helices, with 12 alpha helices folded into an alpha-alpha barrel. This arrangement forms a funnel-shaped cavity in the center of the barrel, where the active sites of GGTase-I is located. This cavity is hydrophobic and contains a number of conserved aromatic residues. The N-terminal domain is disordered and proline-rich, and has no direct influence on the catalytic activity
additional information
the beta subunit is primarily composed of alpha helices that are arranged into different shapes. The beta subunit is an alpha-alpha barrel. The beta subunit of GGTase-I consists of 13 alpha helices, with 12 alpha helices folded into an alpha-alpha barrel. This arrangement forms a funnel-shaped cavity in the center of the barrel, where the active sites of GGTase-I is located. This cavity is hydrophobic and contains a number of conserved aromatic residues. The N-terminal domain is disordered and proline-rich, and has no direct influence on the catalytic activity
additional information
both alpha and beta subunits are composed primarily of alpha helices. The beta subunits of GGTI consist of 13 alpha helices, and 12 of them are folded into an alpha-alpha barrel. The helices of the alpha subunit are arranged in a crescent-shaped superhelix that wraps around the alpha-alpha barrel of beta subunit. This arrangement creates a deep, funnel-shaped cavity in the center of the barrel, and the active sites of GGTI are located within this cavity
additional information
both alpha and beta subunits are composed primarily of alpha helices. The beta subunits of GGTI consist of 13 alpha helices, and 12 of them are folded into an alpha-alpha barrel. The helices of the alpha subunit are arranged in a crescent-shaped superhelix that wraps around the alpha-alpha barrel of beta subunit. This arrangement creates a deep, funnel-shaped cavity in the center of the barrel, and the active sites of GGTI are located within this cavity
additional information
both alpha and beta subunits are composed primarily of alpha helices. The beta subunits of GGTI consist of 13 alpha helices, and 12 of them are folded into an alpha-alpha barrel. The helices of the alpha subunit are arranged in a crescent-shaped superhelix that wraps around the alpha-alpha barrel of beta subunit. This arrangement creates a deep, funnel-shaped cavity in the center of the barrel, and the active sites of GGTI are located within this cavity
additional information
both alpha and beta subunits are composed primarily of alpha helices. The beta subunits of GGTI consist of 13 alpha helices, and 12 of them are folded into an alpha-alpha barrel. The helices of the alpha subunit are arranged in a crescent-shaped superhelix that wraps around the alpha-alpha barrel of beta subunit. This arrangement creates a deep, funnel-shaped cavity in the center of the barrel, and the active sites of GGTI are located within this cavity
additional information
the alpha subunit is primarily composed of alpha helices that are arranged into different shapes. The alpha subunit is a crescent-shaped super helix. The N-terminal domain is disordered and proline-rich, and has no direct influence on the catalytic activity
additional information
the alpha subunit is primarily composed of alpha helices that are arranged into different shapes. The alpha subunit is a crescent-shaped super helix. The N-terminal domain is disordered and proline-rich, and has no direct influence on the catalytic activity
additional information
the beta subunit is primarily composed of alpha helices that are arranged into different shapes. The beta subunit is an alpha-alpha barrel. The beta subunit of GGTase-I consists of 13 alpha helices, with 12 alpha helices folded into an alpha-alpha barrel. This arrangement forms a funnel-shaped cavity in the center of the barrel, where the active sites of GGTase-I is located. This cavity is hydrophobic and contains a number of conserved aromatic residues. The N-terminal domain is disordered and proline-rich, and has no direct influence on the catalytic activity
additional information
the beta subunit is primarily composed of alpha helices that are arranged into different shapes. The beta subunit is an alpha-alpha barrel. The beta subunit of GGTase-I consists of 13 alpha helices, with 12 alpha helices folded into an alpha-alpha barrel. This arrangement forms a funnel-shaped cavity in the center of the barrel, where the active sites of GGTase-I is located. This cavity is hydrophobic and contains a number of conserved aromatic residues. The N-terminal domain is disordered and proline-rich, and has no direct influence on the catalytic activity