4CA4
Crystal structure of FimH lectin domain with the Tyr48Ala mutation, in complex with heptyl alpha-D-mannopyrannoside
Summary for 4CA4
| Entry DOI | 10.2210/pdb4ca4/pdb |
| Descriptor | FIMH, heptyl alpha-D-mannopyranoside (3 entities in total) |
| Functional Keywords | cell adhesion, bacterial adhesin, type 1 fimbriae, urinary tract infection, variable immunoglobulin fold, heptyl mannose, fimh antagonist |
| Biological source | ESCHERICHIA COLI |
| Total number of polymer chains | 2 |
| Total formula weight | 34206.14 |
| Authors | Rabbani, S.,Bouckaert, J.,Zalewski, A.,Preston, R.,Eid, S.,Thompson, A.,Puorger, C.,Glockshuber, R.,Ernst, B. (deposition date: 2013-10-06, release date: 2014-10-29, Last modification date: 2023-12-20) |
| Primary citation | Rabbani, S.,Krammer, E.M.,Roos, G.,Zalewski, A.,Preston, R.,Eid, S.,Zihlmann, P.,Prevost, M.,Lensink, M.F.,Thompson, A.,Ernst, B.,Bouckaert, J. Mutation of Tyr137 of the universal Escherichia coli fimbrial adhesin FimH relaxes the tyrosine gate prior to mannose binding. IUCrJ, 4:7-23, 2017 Cited by PubMed: 28250938DOI: 10.1107/S2052252516016675 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.84 Å) |
Structure validation
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