5I3K
Structure-Function Studies on Role of Hydrophobic Clamping of a Basic Glutamate in Catalysis by Triosephosphate Isomerase
Summary for 5I3K
| Entry DOI | 10.2210/pdb5i3k/pdb |
| Related | 5I3F 5I3G 5I3H 5I3I 5I3J |
| Descriptor | Triosephosphate isomerase, glycosomal, SODIUM 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 | 4 |
| Total formula weight | 107832.07 |
| 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 Cited by PubMed: 27149328DOI: 10.1021/acs.biochem.6b00311 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.209 Å) |
Structure validation
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