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Figure 1 | BMC Biochemistry

Figure 1

From: The role of the C8 proton of ATP in the regulation of phosphoryl transfer within kinases and synthetases

Figure 1

Coordination of ADP and ATP. The coordination of either ADP or ATP in the active sites of (A) shikimate kinase (Accession number, 1L4U), (B) acetate kinase (Accession number, 1TUY), (C) hexokinase (Accession number, 2E2P), (D) phosphofructokinase (Accession number, 3F5M), (E) glutamine synthetase (Accession number, 1F52), and (F) ATP atom numbering. The C8H of the ADP in the active site of shikimate kinase (A) is coordinated to the oxygen of the α-phosphate via Thr17 via a hydrogen bonding network. The C8H of the ADP in the active site of acetate kinase (B) is coordinated to the oxygen of the β-phosphate however, the di-phosphate of the ADP is orientated away from the SO42- which occupies the acetate binding site indicating a distortion in the conformation of the ADP within the active site. The C8H of the ADP is within hydrogen bonding distance of Arg 285 and Asn 335. The C8H of the ADP in the active site of hexokinase kinase (C) is coordinated to the oxygen of the α-phosphate via the guanidium moiety of Arg25. The C8H of the ADP in the active site of phosphofructokinase (D) is directly coordinated to the oxygen of the α-phosphate. The C8H of the ATP in the active site of glutamine synthetase (E) impact on the coordination of the β-phosphate via the coordination to the backbone carbonyl of His271. All inter-atomic distances are as indicated.

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