1FLM
DIMER OF FMN-BINDING PROTEIN FROM DESULFOVIBRIO VULGARIS (MIYAZAKI F)
Summary for 1FLM
| Entry DOI | 10.2210/pdb1flm/pdb |
| Descriptor | PROTEIN (FMN-BINDING PROTEIN), FLAVIN MONONUCLEOTIDE (3 entities in total) |
| Functional Keywords | fmn binding, electron transport |
| Biological source | Desulfovibrio vulgaris str. 'Miyazaki F' |
| Cellular location | Cytoplasm: Q46604 |
| Total number of polymer chains | 2 |
| Total formula weight | 27218.82 |
| Authors | Suto, K.,Kawagoe, K.,Shibata, N.,Morimoto, K.,Higuchi, Y.,Kitamura, M.,Nakaya, T.,Yasuoka, N. (deposition date: 1999-03-10, release date: 2000-03-06, Last modification date: 2023-12-27) |
| Primary citation | Suto, K.,Kawagoe, K.,Shibata, N.,Morimoto, Y.,Higuchi, Y.,Kitamura, M.,Nakaya, T.,Yasuoka, N. How do the x-ray structure and the NMR structure of FMN-binding protein differ? Acta Crystallogr.,Sect.D, 56:368-371, 2000 Cited by PubMed Abstract: The crystal structure of FMN-binding protein (FMN-bp) from Desulfovibrio vulgaris Miyazaki F was solved by the multiple isomorphous replacement method and refined to an R factor of 15.1% at 1.3 A resolution. FMN-bp exists in a dimeric form in the crystal, in contrast to the monomeric structure determined by NMR. R.m.s. deviations between the crystal structure and the solution structure are more than 2 A, which implies significant differences. There are some hydrophobic residues in the interface between the two monomers. In particular, Leu122 in the C-terminus has a close contact with the o-xylene moiety of FMN, while solvent molecules may cover the o-xylene moiety in the solution structure. PubMed: 10713530DOI: 10.1107/S0907444900000111 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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