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. 2014 Jul 24;42(15):9949–9963. doi: 10.1093/nar/gku683

Table 1. Hydrogen bonds formed between the fingers domain loop aspartic acid or its equivalent (the amino acid shown in green and arrowed in Figure 1) and amino acids (shown in blue) in the subsequent α-helix.

DNA polymerase Data source Number of H bonds Hydrogen bonding partnersa
Sce-Pol α pdb, 4FVM 3 D929-H931
D929-K932
D929-R933
Sce-Pol δ pdb, 3IAY 3 D686-F688
D686-K689
D686-R690
Sce-Pol ϵb pdb, 4M8O 1 D807-K811
Sce-Pol ζb ‘Phyre2’ model 2 D1070-T1073
D1070-K1075
Pfu-Pol pdb, 2JGU 2 D473-I475
D473-K477
Pfu-Pol D473Gb ‘Phyre2’ model 1 G473-K477
Tgo-Pol pdb, 1TGO 3 D472-I474
D472-E475
D472-K476
Tgo-Pol Z1b ‘Phyre2’ model 3 D473-T476
D473-K478
D473-R479
Eco-Pol IIc pdb, 3K5O 3 N485-L488
N485-S489
N485-A491

aThe first residue shown is the aspartic acid (asparagine in the case of Eco-Pol II) in the loop region, the second the amino acids in the following α-helix. The underlined hydrogen bonds were found with a distance constraint <0.4 Å and an angle constraint <20°. The other hydrogen bonds had more relaxed constraints of <1 Å and <30°.

bThese DNA polymerases possess a fingers loop that is longer than three amino acids.

cWith Eco-Pol II the third residue in the loop is asparagine rather than aspartic acid.