4QPC
 
 | | Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (Y200A) from zebrafish | | Descriptor: | 10-formyltetrahydrofolate dehydrogenase | | Authors: | Lin, C.C, Chen, C.J, Fu, T.F, Chuankhayan, P, Kao, T.T, Chang, W.N. | | Deposit date: | 2014-06-23 | | Release date: | 2015-04-15 | | Last modified: | 2023-11-08 | | Method: | X-RAY DIFFRACTION (1.902 Å) | | Cite: | Structures of the hydrolase domain of zebrafish 10-formyltetrahydrofolate dehydrogenase and its complexes reveal a complete set of key residues for hydrolysis and product inhibition.
Acta Crystallogr.,Sect.D, 71, 2015
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4TT8
 | | Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with 10-formyl-5,8-dideazafolate | | Descriptor: | 10-formyltetrahydrofolate dehydrogenase, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, N-(4-{[(2-amino-4-hydroxyquinazolin-6-yl)methyl](formyl)amino}benzoyl)-L-glutamic acid | | Authors: | Lin, C.C, Chen, C.J, Fu, T.F, Chuankhayan, P, Kao, T.T, Chang, W.N. | | Deposit date: | 2014-06-20 | | Release date: | 2015-04-15 | | Last modified: | 2023-11-08 | | Method: | X-RAY DIFFRACTION (2.301 Å) | | Cite: | Structures of the hydrolase domain of zebrafish 10-formyltetrahydrofolate dehydrogenase and its complexes reveal a complete set of key residues for hydrolysis and product inhibition.
Acta Crystallogr.,Sect.D, 71, 2015
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4TTS
 | | Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (Y200A) complex with 10-formyl-5,8-dideazafolate | | Descriptor: | 10-formyltetrahydrofolate dehydrogenase, N-(4-{[(2-amino-4-hydroxyquinazolin-6-yl)methyl](formyl)amino}benzoyl)-L-glutamic acid | | Authors: | Lin, C.C, Chen, C.J, Fu, T.F, Chuankhayan, P, Kao, T.T, Chang, W.N. | | Deposit date: | 2014-06-23 | | Release date: | 2015-04-15 | | Last modified: | 2023-11-08 | | Method: | X-RAY DIFFRACTION (2 Å) | | Cite: | Structures of the hydrolase domain of zebrafish 10-formyltetrahydrofolate dehydrogenase and its complexes reveal a complete set of key residues for hydrolysis and product inhibition.
Acta Crystallogr.,Sect.D, 71, 2015
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4TS4
 | | Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) from zebrafish | | Descriptor: | 10-formyltetrahydrofolate dehydrogenase | | Authors: | Lin, C.C, Chen, C.J, Fu, T.F, Chuankhayan, P, Kao, T.T, Chang, W.N. | | Deposit date: | 2014-06-18 | | Release date: | 2015-04-15 | | Last modified: | 2023-11-08 | | Method: | X-RAY DIFFRACTION (1.75 Å) | | Cite: | Structures of the hydrolase domain of zebrafish 10-formyltetrahydrofolate dehydrogenase and its complexes reveal a complete set of key residues for hydrolysis and product inhibition.
Acta Crystallogr.,Sect.D, 71, 2015
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4QPD
 | | Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with tetrahydrofolate | | Descriptor: | (6S)-5,6,7,8-TETRAHYDROFOLATE, 10-formyltetrahydrofolate dehydrogenase, DI(HYDROXYETHYL)ETHER | | Authors: | Lin, C.C, Chen, C.J, Fu, T.F, Chuankhayan, P, Kao, T.T, Chang, W.N. | | Deposit date: | 2014-06-23 | | Release date: | 2015-04-15 | | Last modified: | 2024-03-20 | | Method: | X-RAY DIFFRACTION (2.1 Å) | | Cite: | Structures of the hydrolase domain of zebrafish 10-formyltetrahydrofolate dehydrogenase and its complexes reveal a complete set of key residues for hydrolysis and product inhibition.
Acta Crystallogr.,Sect.D, 71, 2015
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4R8V
 | | Crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase (wild-type) complex with formate | | Descriptor: | 10-formyltetrahydrofolate dehydrogenase, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, DI(HYDROXYETHYL)ETHER, ... | | Authors: | Lin, C.C, Chen, C.J, Fu, T.F, Chuankhayan, P, Kao, T.T, Chang, W.N. | | Deposit date: | 2014-09-03 | | Release date: | 2015-04-15 | | Last modified: | 2023-11-08 | | Method: | X-RAY DIFFRACTION (2.197 Å) | | Cite: | Structures of the hydrolase domain of zebrafish 10-formyltetrahydrofolate dehydrogenase and its complexes reveal a complete set of key residues for hydrolysis and product inhibition.
Acta Crystallogr.,Sect.D, 71, 2015
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