2ZZI
Crystal structure of TTHA1623 in a di-iron-bound form
Summary for 2ZZI
| Entry DOI | 10.2210/pdb2zzi/pdb |
| Related | 2ZWR |
| Descriptor | Metallo-beta-lactamase superfamily protein, FE (III) ION, ACETATE ION, ... (4 entities in total) |
| Functional Keywords | metallo-beta-lactamase, hydrolase |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 2 |
| Total formula weight | 44984.76 |
| Authors | Yamamura, A.,Okada, A.,Kameda, Y.,Ohtsuka, J.,Nakagawa, N.,Ebihara, A.,Yokoyama, S.,Kuramitsu, S.,Nagata, K.,Tanokura, M. (deposition date: 2009-02-16, release date: 2010-01-05, Last modification date: 2023-11-01) |
| Primary citation | Yamamura, A.,Okada, A.,Kameda, Y.,Ohtsuka, J.,Nakagawa, N.,Ebihara, A.,Nagata, K.,Tanokura, M. Structure of TTHA1623, a novel metallo-beta-lactamase superfamily protein from Thermus thermophilus HB8 Acta Crystallogr.,Sect.F, 65:455-459, 2009 Cited by PubMed Abstract: TTHA1623 is a metallo-beta-lactamase superfamily protein from the extremely thermophilic bacterium Thermus thermophilus HB8. Homologues of TTHA1623 exist in a wide range of bacteria and archaea and one eukaryote, Giardia lamblia, but their function remains unknown. To analyze the structural properties of TTHA1623, the crystal structures of its iron-bound and zinc-bound forms have been determined to 2.8 and 2.2 A resolution, respectively. TTHA1623 possesses an alphabetabetaalpha-fold similar to that of other metallo-beta-lactamase superfamily proteins with glyoxalase II-type metal coordination. However, TTHA1623 exhibits a putative substrate-binding pocket with a unique shape. PubMed: 19407375DOI: 10.1107/S174430910901361X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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