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PDB: 6 results

5I3F
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BU of 5i3f by Molmil
Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase
Descriptor: Triosephosphate isomerase, glycosomal
Authors:Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J.
Deposit date:2016-02-10
Release date:2016-05-18
Last modified:2023-09-27
Method:X-RAY DIFFRACTION (1.72 Å)
Cite:Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
Biochemistry, 55, 2016
5I3H
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BU of 5i3h by Molmil
Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase
Descriptor: 2-PHOSPHOGLYCOLIC ACID, POTASSIUM ION, Triosephosphate isomerase, ...
Authors:Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J.
Deposit date:2016-02-10
Release date:2016-05-18
Last modified:2023-09-27
Method:X-RAY DIFFRACTION (2.25 Å)
Cite:Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
Biochemistry, 55, 2016
5I3J
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BU of 5i3j by Molmil
Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase
Descriptor: SODIUM ION, Triosephosphate isomerase, glycosomal
Authors:Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J.
Deposit date:2016-02-10
Release date:2016-05-18
Last modified:2023-09-27
Method:X-RAY DIFFRACTION (1.8 Å)
Cite:Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
Biochemistry, 55, 2016
5I3I
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BU of 5i3i by Molmil
Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase
Descriptor: 2-PHOSPHOGLYCOLIC ACID, Triosephosphate isomerase, glycosomal
Authors:Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J.
Deposit date:2016-02-10
Release date:2016-05-18
Last modified:2023-09-27
Method:X-RAY DIFFRACTION (2.2 Å)
Cite:Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
Biochemistry, 55, 2016
5I3G
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BU of 5i3g by Molmil
Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase
Descriptor: Triosephosphate isomerase, glycosomal
Authors:Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J.
Deposit date:2016-02-10
Release date:2016-05-18
Last modified:2023-09-27
Method:X-RAY DIFFRACTION (1.96 Å)
Cite:Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
Biochemistry, 55, 2016
5I3K
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BU of 5i3k by Molmil
Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase
Descriptor: 2-PHOSPHOGLYCOLIC ACID, SODIUM ION, Triosephosphate isomerase, ...
Authors:Drake, E.J, Gulick, A.M, Richard, J.P, Zhai, X, Kim, K, Reinhardt, C.J.
Deposit date:2016-02-10
Release date:2016-05-18
Last modified:2023-09-27
Method:X-RAY DIFFRACTION (2.209 Å)
Cite:Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.
Biochemistry, 55, 2016

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