1fvp | pdb_00001fvp

FLAVOPROTEIN 390

spinqualitylabelsall models 1fvp, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1fvp is a 2 chain structure with sequence from "acinetobacter_phosphorescens"_brisou_1955 "acinetobacter phosphorescens" brisou 1955. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: FMA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The three-dimensional structure of a flavoprotein, FP(390), from a luminescent bacterium, Photobacterium phosphoreum, solved by the molecular-replacement method, was refined to an R factor of 24.0% for 17 433 independent reflections, from 6.0 to 2.7 A resolution, collected by synchrotron radiation. The asymmetric unit of the crystal (space group P4(3)22, a = b = 76.8 and c = 242 A) contains two monomer molecules related by a non-crystallographic twofold axis to form a dimer. There are two Q-flavin [flavin mononucleotide (FMN) with myristic acid] molecules in FP(390) monomer. One of them is located at the interface of dimer which is bound to both monomer and the another is at the molecular surface. The electron density of myristic acids of Q-flavins at the dimer interface in both monomer are weak and unclear, showing the possibility that the Q-flavins bound in this site are not a single species but a mixture of two components, 6-(3"-myristic acid)-FMN and 6-(4"- myristic acid)-FMN. Structure of flavoprotein FP390 from a luminescent bacterium Photobacterium phosphoreum refined at 2.7 A resolution.,Kita A, Kasai S, Miyata M, Miki K Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):77-86. PMID:15299728 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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