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5O8I
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CRYSTAL STRUCTURE OF HUMAN HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN 1 (HHINT1) CRYSTALLIZED AT P212121 SPACE GROUP, AND REFINED TO 1.27 A
Descriptor:Histidine triad nucleotide-binding protein 1, ADENOSINE-5'-DIPHOSPHATE
Authors:Dolot, R.M., Seda, A., Nawrot, B.C.
Deposit date:2017-06-13
Release date:2017-06-28
Method:X-RAY DIFFRACTION (1.27 Å)
Cite:Differences in crystal packing as the key factor for stabilization of the N-terminal fragment of hHINT1 protein
To Be Published
6G9Z
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CRYSTAL STRUCTURE OF HUMAN HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN 1 (HHINT1) CRYSTALLIZED AT P212121 SPACE GROUP, WITH VISIBLE EXTENDED FRAGMENT OF N-TERMINUS
Descriptor:Histidine triad nucleotide-binding protein 1, (2S)-2-hydroxybutanedioic acid
Authors:Dolot, R.M., Seda, A., Nawrot, B.C.
Deposit date:2018-04-11
Release date:2018-04-18
Method:X-RAY DIFFRACTION (1.43 Å)
Cite:Differences in crystal packing as the key factor for stabilization of the N-terminal fragment of hHINT1 protein
To Be Published
6YI0
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HUMAN HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN 2 (HHINT2) REFINED TO 1.65 A IN P41212 SPACE GROUP
Descriptor:Histidine triad nucleotide-binding protein 2, mitochondrial, SODIUM ION
Authors:Dolot, R.D., Wlodarczyk, A., Bujacz, G.D., Nawrot, B.C.
Deposit date:2020-03-31
Release date:2020-04-29
Method:X-RAY DIFFRACTION (1.65 Å)
Cite:The histidine nucleotide-binding protein 2 forms a complex with the non-hydrolyzable analogue of Ap4A -biochemical, biophysical and structural studies of the enzyme.
To Be Published
6YPR
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HUMAN HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN 2 (HHINT2) REFINED TO 1.26 A IN H32 SPACE GROUP
Descriptor:Histidine triad nucleotide-binding protein 2, mitochondrial, GLYCEROL
Authors:Dolot, R.D., Wlodarczyk, A., Bujacz, G.D., Nawrot, B.C.
Deposit date:2020-04-16
Release date:2020-04-29
Method:X-RAY DIFFRACTION (1.26 Å)
Cite:The histidine nucleotide-binding protein 2 forms a complex with the non-hydrolyzable analogue of Ap4A -biochemical, biophysical and structural studies of the enzyme.
To be published
6YPX
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HUMAN HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN 2 (HHINT2) REFINED TO 2.11 A IN C2221 SPACE GROUP
Descriptor:Histidine triad nucleotide-binding protein 2, mitochondrial, CACODYLATE ION, ...
Authors:Dolot, R.D., Wlodarczyk, A., Bujacz, G.D., Nawrot, B.C.
Deposit date:2020-04-16
Release date:2020-04-29
Method:X-RAY DIFFRACTION (2.11 Å)
Cite:The histidine nucleotide-binding protein 2 forms a complex with the non-hydrolyzable analogue of Ap4A -biochemical, biophysical and structural studies of the enzyme.
To Be Published
6YQD
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HUMAN HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN 2 (HHINT2) REFINED TO 1.41 A IN P212121 SPACE GROUP
Descriptor:Histidine triad nucleotide-binding protein 2, mitochondrial, POTASSIUM ION
Authors:Dolot, R.D., Wlodarczyk, A., Bujacz, G.D., Nawrot, B.C.
Deposit date:2020-04-16
Release date:2020-04-29
Method:X-RAY DIFFRACTION (1.407 Å)
Cite:The histidine nucleotide-binding protein 2 forms a complex with the non-hydrolyzable analogue of Ap4A -biochemical, biophysical and structural studies of the enzyme.
To be published
6YQM
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HUMAN HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN 1 (HHINT1) COMPLEXED WITH DGMP AND REFINED TO 1.02 A
Descriptor:Histidine triad nucleotide-binding protein 1, 2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE, DI(HYDROXYETHYL)ETHER
Authors:Dolot, R.D., Seda, A., Nawrot, B.C.
Deposit date:2020-04-17
Release date:2020-04-29
Method:X-RAY DIFFRACTION (1.02 Å)
Cite:The histidine nucleotide-binding protein 2 forms a complex with the non-hydrolyzable analogue of Ap4A -biochemical, biophysical and structural studies of the enzyme.
To Be Published
6YVP
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HUMAN HISTIDINE TRIAD NUCLEOTIDE-BINDING PROTEIN 2 (HHINT2) COMPLEXED WITH DGMP AND REFINED TO 2.77 A
Descriptor:Histidine triad nucleotide-binding protein 2, mitochondrial, 2'-DEOXYGUANOSINE-5'-MONOPHOSPHATE
Authors:Dolot, R.D., Krakowiak, A., Nawrot, B.C.
Deposit date:2020-04-28
Release date:2020-05-13
Method:X-RAY DIFFRACTION (2.77 Å)
Cite:The histidine nucleotide-binding protein 2 forms a complex with the non-hydrolyzable analogue of Ap4A -biochemical, biophysical and structural studies of the enzyme.
To Be Published