2bt3 | pdb_00002bt3

AGAO IN COMPLEX WITH RUTHENIUM-C4-WIRE AT 1.73 ANGSTROMS

spinqualitylabelsall models 2bt3, resolution 1.73Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2bt3 is a 1 chain structure with sequence from "achromobacter_globiformis"_(conn_1928)_bergey_et_al._1930 "achromobacter globiformis" (conn 1928) bergey et al. 1930. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CU, GOL, NA, R4A, SO4 NonStd Res: TPQ Related: 1av4, 1avk, 1avl, 1iqx, 1iqy, 1iu7, 1ivu, 1ivv, 1ivw, 1ivx, 1rjo, 1sih, 1sii, 1ui7, 1ui8, 1w4n, 1w5z, 1w6c, 1w6g Activity: Oxidoreductase, with EC number and 1.4.3.22 1.4.3.21 and 1.4.3.22 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum 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 Molecular wires comprising a Ru(II)- or Re(I)-complex head group, an aromatic tail group, and an alkane linker reversibly inhibit the activity of the copper amine oxidase from Arthrobacter globiformis (AGAO), with K(i) values between 6 muM and 37 nM. In the crystal structure of a Ru(II)-wire:AGAO conjugate, the wire occupies the AGAO active-site substrate access channel, the trihydroxyphenylalanine quinone cofactor is ordered in the "off-Cu" position with its reactive carbonyl oriented toward the inhibitor, and the "gate" residue, Tyr-296, is in the "open" position. Head groups, tail-group substituents, and linker lengths all influence wire-binding interactions with the enzyme. Reversible inhibition of copper amine oxidase activity by channel-blocking ruthenium(II) and rhenium(I) molecular wires.,Contakes SM, Juda GA, Langley DB, Halpern-Manners NW, Duff AP, Dunn AR, Gray HB, Dooley DM, Guss JM, Freeman HC Proc Natl Acad Sci U S A. 2005 Sep 20;102(38):13451-6. Epub 2005 Sep 12. PMID:16157884 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Copper Amine Oxidase

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