1I0E
CRYSTAL STRUCTURE OF CREATINE KINASE FROM HUMAN MUSCLE
Summary for 1I0E
| Entry DOI | 10.2210/pdb1i0e/pdb |
| Descriptor | CREATINE KINASE,M CHAIN (1 entity in total) |
| Functional Keywords | double helix, dimer, transferase |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 172680.55 |
| Authors | Shen, Y.-Q.,Tang, L.,Zhou, H.-M.,Lin, Z.-J. (deposition date: 2001-01-29, release date: 2003-04-01, Last modification date: 2024-04-03) |
| Primary citation | Shen, Y.Q.,Tang, L.,Zhou, H.M.,Lin, Z.J. Structure of human muscle creatine kinase. Acta Crystallogr.,Sect.D, 57:1196-1200, 2001 Cited by PubMed Abstract: The crystal structure of human muscle creatine kinase has been determined by the molecular-replacement method and refined at 3.5A resolution. The structures of both the monomer and the dimer closely resemble those of the other known structures in the creatine kinase family. Two types of dimers, one with a non-crystallographic twofold symmetry axis and the other with a crystallographic twofold symmetry axis, were found to exist simultaneously in the crystal. These dimers form an infinite "double-helix"-like structure along an unusual long crystallographic 3(1) axis. PubMed: 11517911DOI: 10.1107/s0907444901007703 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.5 Å) |
Structure validation
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