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PDB: 4 results
4KH5
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BU of 4kh5 by Molmil
Toxoplasma gondii NTPDase1 C258S/C268S in complex with Mg and AMPNP
Descriptor: 5'-O-[(R)-hydroxy(phosphonoamino)phosphoryl]adenosine, MAGNESIUM ION, Nucleoside-triphosphatase 2
Authors:Krug, U, Totzauer, R, Strater, N.
Deposit date:2013-04-30
Release date:2013-11-06
Last modified:2017-11-15
Method:X-RAY DIFFRACTION (3 Å)
Cite:The ATP/ADP substrate specificity switch between Toxoplasma gondii NTPDase1 and NTPDase3 is caused by an altered mode of binding of the substrate base.
Chembiochem, 14, 2013
4KH6
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BU of 4kh6 by Molmil
Toxoplasma gondii NTPDase1 C258S/C268S E493G crystallized with Mg and AMPNP
Descriptor: 5'-O-[(R)-hydroxy(phosphonoamino)phosphoryl]adenosine, MAGNESIUM ION, Nucleoside-triphosphatase 2
Authors:Krug, U, Totzauer, R, Strater, N.
Deposit date:2013-04-30
Release date:2013-11-06
Last modified:2017-11-15
Method:X-RAY DIFFRACTION (2.4 Å)
Cite:The ATP/ADP substrate specificity switch between Toxoplasma gondii NTPDase1 and NTPDase3 is caused by an altered mode of binding of the substrate base.
Chembiochem, 14, 2013
4JEP
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BU of 4jep by Molmil
Crystal structure of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 1 (NTPDase1)
Descriptor: Nucleoside-triphosphatase 2
Authors:Krug, U, Totzauer, R, Strater, N.
Deposit date:2013-02-27
Release date:2013-04-10
Last modified:2017-11-15
Method:X-RAY DIFFRACTION (3.1 Å)
Cite:The crystal structure of Toxoplasma gondii nucleoside triphosphate diphosphohydrolase 1 represents a conformational intermediate in the reductive activation mechanism of the tetrameric enzyme.
Proteins, 81, 2013
4KH4
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BU of 4kh4 by Molmil
Toxoplasma gondii NTPDase1 C258S/C268S in complex with Mg and AMPPNP
Descriptor: MAGNESIUM ION, Nucleoside-triphosphatase 2, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
Authors:Krug, U, Totzauer, R, Strater, N.
Deposit date:2013-04-30
Release date:2013-11-06
Last modified:2017-11-15
Method:X-RAY DIFFRACTION (3 Å)
Cite:The ATP/ADP substrate specificity switch between Toxoplasma gondii NTPDase1 and NTPDase3 is caused by an altered mode of binding of the substrate base.
Chembiochem, 14, 2013

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