1hpk
From Proteopedia
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SOLUTION NMR STRUCTURE OF THE HUMAN PLASMINOGEN KRINGLE 1 DOMAIN COMPLEXED WITH 6-AMINOHEXANOIC ACID AT PH 5.3, 310K, DERIVED FROM RANDOMLY GENERATED STRUCTURES USING SIMULATED ANNEALING, MINIMIZED AVERAGE STRUCTURE
Overview
The solution structure of the human plasminogen kringle 1 domain complexed, to the antifibrinolytic drug 6-aminohexanoic acid (epsilon Ahx) was, obtained on the basis of 1H-NMR spectroscopic data and dynamical simulated, annealing calculations. Two sets of structures were derived starting from, (a) random coil conformations and (b) the (mutated) crystallographic, structure of the homologous prothrombin kringle 1. The two sets display, essentially the same backbone folding (pairwise root-mean-square, deviation, 0.15 nm) indicating that, regardless of the initial structure, the data is sufficient to locate a conformation corresponding to an, essentially unique energy minimum. The conformations of residues connected, to prolines were localized to energetically preferred regions of the, ... [(full description)]
About this Structure
1HPK is a [Single protein] structure of sequence from [Homo sapiens] with ACA as [ligand]. Active as [[1]], with EC number [3.4.21.7]. Full crystallographic information is available from [OCA].
Reference
Solution structure of the epsilon-aminohexanoic acid complex of human plasminogen kringle 1., Rejante MR, Llinas M, Eur J Biochem. 1994 May 1;221(3):939-49. PMID:8181476
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