2ah0 | pdb_00002ah0

Crystal structure of the carbinolamine intermediate in the reductive half-reaction of aromatic amine dehydrogenase (AADH) with tryptamine. Monoclinic form

spinqualitylabelsall models 2ah0, resolution 1.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2ah0 is a 4 chain structure with sequence from Alcaligenes faecalis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: TSC, TSH NonStd Res: TRQ Related: 2agl, 2agu, 2agw, 2agx, 2agy, 2agz, 2ah1 Activity: Aralkylamine dehydrogenase (azurin), with EC number 1.4.9.2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AAUA_ALCFA] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor. [AAUB_ALCFA] Oxidizes primary aromatic amines and, more slowly, some long-chain aliphatic amines, but not methylamine or ethylamine. Uses azurin as an electron acceptor to transfer electrons from the reduced tryptophylquinone cofactor. 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 We present an atomic-level description of the reaction chemistry of an enzyme-catalyzed reaction dominated by proton tunneling. By solving structures of reaction intermediates at near-atomic resolution, we have identified the reaction pathway for tryptamine oxidation by aromatic amine dehydrogenase. Combining experiment and computer simulation, we show proton transfer occurs predominantly to oxygen O2 of Asp(128)beta in a reaction dominated by tunneling over approximately 0.6 angstroms. The role of long-range coupled motions in promoting tunneling is controversial. We show that, in this enzyme system, tunneling is promoted by a short-range motion modulating proton-acceptor distance and no long-range coupled motion is required. Atomic description of an enzyme reaction dominated by proton tunneling.,Masgrau L, Roujeinikova A, Johannissen LO, Hothi P, Basran J, Ranaghan KE, Mulholland AJ, Sutcliffe MJ, Scrutton NS, Leys D Science. 2006 Apr 14;312(5771):237-41. PMID:16614214 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Aromatic amine dehydrogenase 3D structures

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