5I3H

Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase

Summary for 5I3H

• Entry DOI: 10.2210/pdb5i3h/pdb
• Related: 5I3F 5I3G 5I3I 5I3J 5I3K
• Descriptor: Triosephosphate isomerase, glycosomal, POTASSIUM ION, 2-PHOSPHOGLYCOLIC ACID, ... (4 entities in total)
• Functional Keywords: triosephosphate isomerase, catalysis, hydrophobic clamping, pga, isomerase
• Biological source: Trypanosoma brucei brucei
• Cellular location: Glycosome: P04789
• Total number of polymer chains: 2
• Total formula weight: 53797.57

Authors

Drake, E.J.,Gulick, A.M.,Richard, J.P.,Zhai, X.,Kim, K.,Reinhardt, C.J. (deposition date: 2016-02-10, release date: 2016-05-18, Last modification date: 2023-09-27)

• Primary citation: Richard, J.P.,Amyes, T.L.,Malabanan, M.M.,Zhai, X.,Kim, K.J.,Reinhardt, C.J.,Wierenga, R.K.,Drake, E.J.,Gulick, A.M.; Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase.; Biochemistry, 55:3036-3047, 2016; PubMed: 27149328; DOI: 10.1021/acs.biochem.6b00311

Experimental method

X-RAY DIFFRACTION (2.25 Å)