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. 2005 Apr;14(4):1104–1114. doi: 10.1110/ps.041153605

Table 3.

Ligand-free structures and their corresponding ligand-bound complexes used in testing the minimal rotation hypothesis

PDB code Resolution (Å) Best ligand RMSD (Å)
No. Free Bound Protein/ligand complex Free Bound Flexible docking Rigid docking Template size
1M 1ahc 1ahb Alpha-momorcharin/Formycin 5′-monophosphate 2.0 2.2 0.94 88
2M 1ajz 1aj2 Dihydropteroate synthase/Dihydropterine-diphosphate 2.0 2.0 0.75 79
3 3cox 1coy Cholesterol oxidase/3-beta-hydroxy-5-androsten-17-one 1.8 1.8 1.61 74
4 1gmq 1gmr RNAse SA/Guanosine-2′-monophosphate 1.8 1.8 1.28 1.63 87
5 3grs 1gra Glutathione reductase/Glutathione disulfide 1.5 2.0 0.69 1.88 139
6 1kem 1kel Catalytic antibody 28B4 FAB Fragment/AAHa 2.2 1.9 0.46 74
7M 2hvm 1llo Hevamine(endochitinase)/N-Acetyl-d-allosamine 1.8 1.9 0.67 150
8 1nsb 1nsc Neuraminidase/N-acetyl neuraminic acid(sialic acid) 2.2 1.7 0.40 0.67 74
9 1swa 1swd Streptavidin/Biotin 2.0 1.9 0.62 0.67 37
10M 2ptn 1tps Trypsin/Inhibitor A90720A 1.5 1.9 0.93 143
11 1xib 1xid D-Xylose isomerase/L-Ascorbic acid 1.6 1.7 2.28 45
12M 1ydc 1ydb Carbonic anhydrase II/Acetazolamide 2.0 1.9 1.42 50
13 2chs 2cht Chorismate mutase/Endo-oxabicyclic inhibitor 1.9 2.2 1.02 39
14 2apr 3apr Acid proteinase/Reduced peptide inhibitor 1.8 1.8 0.54 153
15 1tli 3tmn Thermolysin/VAL-TRP 2.0 1.7 0.99 0.99 75
16 2ctv 5cna Concanavalin A/alpha-methyl-D-mannopyranoside 2.0 2.0 1.99 57
17 2sga 5sga Proteinase A/Tetrapeptide ACE-PRO-ALA-PRO-TYR 1.5 1.8 0.59 1.90 126
18M 6taa 7taa Fam. 13 alpha amylase/Modified acarbose hexasaccharide 2.1 2.0 0.82 133

The template sizes are given as the number of template points to indicate the differences in the sizes of the binding sites of the proteins.

a AAH = 1-[N-4′-nitrobenzyl-N-4′-carboxybutylaminomethylphosphonic acid.

M Proteins existing as biological monomers both in their ligand-free and ligand-bound states.