6CDZ
 
 | | E. coli thymidylate synthase mutant I264Am | | Descriptor: | 10-PROPARGYL-5,8-DIDEAZAFOLIC ACID, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, 2'-deoxy-5'-uridylic acid, ... | | Authors: | Finer-moore, J.S, Lee, T.T, Stroud, R.M. | | Deposit date: | 2018-02-09 | | Release date: | 2018-05-16 | | Last modified: | 2024-10-16 | | Method: | X-RAY DIFFRACTION (2.4 Å) | | Cite: | A Single Mutation Traps a Half-Sites Reactive Enzyme in Midstream, Explaining Asymmetry in Hydride Transfer.
Biochemistry, 57, 2018
|
|
2NG1
 | | N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS | | Descriptor: | 1,2-ETHANEDIOL, 1,4-DIETHYLENE DIOXIDE, GUANOSINE-5'-DIPHOSPHATE, ... | | Authors: | Freymann, D.M, Stroud, R.M, Walter, P. | | Deposit date: | 1998-09-11 | | Release date: | 1999-07-30 | | Last modified: | 2024-05-22 | | Method: | X-RAY DIFFRACTION (2.02 Å) | | Cite: | Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP.
Nat.Struct.Biol., 6, 1999
|
|
1JMG
 | |
1JMF
 | |
1JMH
 | |
1JMI
 | |
4GEV
 | | E. coli thymidylate synthase Y209W variant in complex with substrate and a cofactor analog | | Descriptor: | 10-PROPARGYL-5,8-DIDEAZAFOLIC ACID, 2'-deoxy-5'-uridylic acid, Thymidylate synthase | | Authors: | Newby, Z, Lee, T.T, Finer-Moore, J, Stroud, R.M. | | Deposit date: | 2012-08-02 | | Release date: | 2012-08-29 | | Last modified: | 2017-11-15 | | Method: | X-RAY DIFFRACTION (1.3 Å) | | Cite: | A remote mutation affects the hydride transfer by disrupting concerted protein motions in thymidylate synthase.
J.Am.Chem.Soc., 134, 2012
|
|
2TGD
 | |
2TSC
 | | STRUCTURE, MULTIPLE SITE BINDING, AND SEGMENTAL ACCOMODATION IN THYMIDYLATE SYNTHASE ON BINDING D/UMP AND AN ANTI-FOLATE | | Descriptor: | 10-PROPARGYL-5,8-DIDEAZAFOLIC ACID, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, THYMIDYLATE SYNTHASE | | Authors: | Montfort, W.R, Stroud, R.M. | | Deposit date: | 1991-07-03 | | Release date: | 1991-10-15 | | Last modified: | 2024-10-16 | | Method: | X-RAY DIFFRACTION (1.97 Å) | | Cite: | Structure, multiple site binding, and segmental accommodation in thymidylate synthase on binding dUMP and an anti-folate.
Biochemistry, 29, 1990
|
|
1TGN
 | |
1NCE
 | | Crystal structure of a ternary complex of E. coli thymidylate synthase D169C with dUMP and the antifolate CB3717 | | Descriptor: | 10-PROPARGYL-5,8-DIDEAZAFOLIC ACID, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, Thymidylate synthase | | Authors: | Birdsall, D.L, Finer-Moore, J, Stroud, R.M. | | Deposit date: | 2002-12-05 | | Release date: | 2002-12-25 | | Last modified: | 2023-08-16 | | Method: | X-RAY DIFFRACTION (2.4 Å) | | Cite: | The only active mutant of thymidylate synthase D169, a residue far from the
site of methyl transfer, demonstrates the exquisite nature of enzyme
specificity.
Protein Eng., 16, 2003
|
|
1SJS
 | |
1TSX
 | | THYMIDYLATE SYNTHASE R179E MUTANT | | Descriptor: | 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, THYMIDYLATE SYNTHASE | | Authors: | Finer-Moore, J, Stroud, R.M. | | Deposit date: | 1995-12-05 | | Release date: | 1996-03-08 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.5 Å) | | Cite: | Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase.
Protein Eng., 9, 1996
|
|
1DNA
 | | D221(169)N MUTANT DOES NOT PROMOTE OPENING OF THE COFACTOR IMIDAZOLIDINE RING | | Descriptor: | 10-PROPARGYL-5,8-DIDEAZAFOLIC ACID, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, THYMIDYLATE SYNTHASE | | Authors: | Sage, C.R, Michelitsch, M.D, Finer-Moore, J, Stroud, R.M. | | Deposit date: | 1998-06-25 | | Release date: | 1998-11-04 | | Last modified: | 2024-10-30 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | D221 in thymidylate synthase controls conformation change, and thereby opening of the imidazolidine.
Biochemistry, 37, 1998
|
|
1TVU
 | |
1NJB
 | | THYMIDYLATE SYNTHASE | | Descriptor: | 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, THYMIDYLATE SYNTHASE | | Authors: | Finer-Moore, J, Stroud, R.M. | | Deposit date: | 1996-01-23 | | Release date: | 1996-10-14 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.74 Å) | | Cite: | Partitioning roles of side chains in affinity, orientation, and catalysis with structures for mutant complexes: asparagine-229 in thymidylate synthase.
Biochemistry, 35, 1996
|
|
1NJA
 | | THYMIDYLATE SYNTHASE, MUTATION, N229C WITH 2'-DEOXYCYTIDINE 5'-MONOPHOSPHATE (DCMP) | | Descriptor: | 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE, THYMIDYLATE SYNTHASE | | Authors: | Finer-Moore, J, Stroud, R.M. | | Deposit date: | 1996-01-23 | | Release date: | 1996-07-11 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.5 Å) | | Cite: | Partitioning roles of side chains in affinity, orientation, and catalysis with structures for mutant complexes: asparagine-229 in thymidylate synthase.
Biochemistry, 35, 1996
|
|
1NJC
 | | THYMIDYLATE SYNTHASE, MUTATION, N229D WITH 2'-DEOXYCYTIDINE 5'-MONOPHOSPHATE (DCMP) | | Descriptor: | 2'-DEOXYCYTIDINE-5'-MONOPHOSPHATE, THYMIDYLATE SYNTHASE | | Authors: | Finer-Moore, J, Stroud, R.M. | | Deposit date: | 1996-01-23 | | Release date: | 1996-07-11 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.5 Å) | | Cite: | Partitioning roles of side chains in affinity, orientation, and catalysis with structures for mutant complexes: asparagine-229 in thymidylate synthase.
Biochemistry, 35, 1996
|
|
1NJD
 | | THYMIDYLATE SYNTHASE, MUTATION, N229D WITH 2'-DEOXYURIDINE 5'-MONOPHOSPHATE (DUMP) | | Descriptor: | 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, THYMIDYLATE SYNTHASE | | Authors: | Finer-Moore, J, Stroud, R.M. | | Deposit date: | 1996-01-23 | | Release date: | 1996-07-11 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | Partitioning roles of side chains in affinity, orientation, and catalysis with structures for mutant complexes: asparagine-229 in thymidylate synthase.
Biochemistry, 35, 1996
|
|
1TRG
 | | E. COLI THYMIDYLATE SYNTHASE IN SYMMETRIC COMPLEX WITH CB3717 AND 2'-DEOXYURIDINE 5'-MONOPHOSPHATE (DUMP) | | Descriptor: | 10-PROPARGYL-5,8-DIDEAZAFOLIC ACID, 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, THYMIDYLATE SYNTHASE | | Authors: | Stout, T.J, Sage, C.R, Stroud, R.M. | | Deposit date: | 1998-05-21 | | Release date: | 1998-08-12 | | Last modified: | 2023-08-09 | | Method: | X-RAY DIFFRACTION (1.9 Å) | | Cite: | The additivity of substrate fragments in enzyme-ligand binding.
Structure, 6, 1998
|
|
1NJE
 | |
1TSY
 | | THYMIDYLATE SYNTHASE R179K MUTANT | | Descriptor: | 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, THYMIDYLATE SYNTHASE | | Authors: | Finer-Moore, J, Stroud, R.M. | | Deposit date: | 1995-12-05 | | Release date: | 1996-03-08 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.2 Å) | | Cite: | Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase.
Protein Eng., 9, 1996
|
|
1TSV
 | | THYMIDYLATE SYNTHASE R179A MUTANT | | Descriptor: | 2'-DEOXYURIDINE 5'-MONOPHOSPHATE, THYMIDYLATE SYNTHASE | | Authors: | Finer-Moore, J, Stroud, R.M. | | Deposit date: | 1995-12-05 | | Release date: | 1996-03-08 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.9 Å) | | Cite: | Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase.
Protein Eng., 9, 1996
|
|
1TVV
 | |
1TSW
 | | THYMIDYLATE SYNTHASE R179A MUTANT | | Descriptor: | PHOSPHATE ION, THYMIDYLATE SYNTHASE | | Authors: | Finer-Moore, J, Stroud, R.M. | | Deposit date: | 1995-12-05 | | Release date: | 1996-03-08 | | Last modified: | 2024-02-14 | | Method: | X-RAY DIFFRACTION (2.5 Å) | | Cite: | Contribution of a salt bridge to binding affinity and dUMP orientation to catalytic rate: mutation of a substrate-binding arginine in thymidylate synthase.
Protein Eng., 9, 1996
|
|
