Refinement of the structure of human basic fibroblast growth factor at 1.6 Å resolution and analysis of presumed heparin binding sites by selenate substitution

The three‐dimensional structure of human basic fibroblast growth factor has been refined to a crystallographic residual of 16.1% at 1.6 Å resolution. The structure has a Kunitz‐type fold and is composed of 12 antiparallel β‐strands, 6 of which form a β‐barrel. One bound sulfate ion has been identified in the model, hydrogen bonded to the side chains of Asn 27, Arg 120, and Lys 125. The side chain of Arg 120 has two conformations, both of which permit hydrogen bonds to the sulfate. This sulfate binding site has been suggested as the binding site for heparin (Eriksson, A.E., Cousens, L.S., Weaver, L.H., & Matthews, B.W., 1991, Proc. Natl. Acad. Sci. USA 88, 3441–3445). Two β‐mercaptoethanol (BME) molecules are also included in the model, each forming a disulfide bond to the Sγ atoms of Cys 69 and Cys 92, respectively. The side chain of Cys 92 has two conformations of which only one can bind BME. Therefore the BME molecule is half occupied at this site.

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