Table 1. Dataset of enzymes with functional loops that close over the active site.
| RMSD (Å) | ||||||
| Enzyme | Number of residuesa | Loop residues | Overall proteinb | Loopc | Isolated loopd | Loop tip motion (Å) |
| Protein Tyr phosphatase (PTP) | 305 | 352–361 | 0.9 | 3.5 | 1.0 | 7.0 |
| HhaI methyltransferase | 327 | 80–100 | 3.9 | 14.5 | 5.3 | 25.0 |
| OMP decarboxylase | 267 (x2) | 203–218 | 2.7 | 9.6 | 4.0 | 14.7 |
| β 1,4-galactosyltransferase | 288 | 345–365 | 3.4 | 11.6 | 5.5 | 21.5 |
| L-lactate dehydrogenase | 317 (x4) | 81–91 | 0.9 | 4.3 | 1.0 | 6.7 |
| 3-dehydroquinase | 252 (x2) | 227–239 | 1.2 | 5.1 | 1.6 | 10.1 |
| Biphosphate aldoase | 307 (x2) | 176–191 | 1.8 | 7.2 | 3.3 | 16.5 |
| Triosephosphate isomerase (TIM) | 248 (x2) | 166–176 | 1.0 | 4.5 | 1.1 | 7.9 |
| Enolase | 436 (x2) | 34–50 | 0.9 | 3.7 | 2.8 | 8.8 |
| Pyruvate mutase | 295 (x4) | 118–134 | 2.4 | 9.7 | 4.2 | 18.0 |
a
Oligomerization state (number of monomers) is specified in parentheses.
b
RMSD between the representative open (apo) and closed (liganded) structures listed in Table S1 in Text S1, based on Cα atoms.
c
RMSD of the loop region calculated after aligning the same apo and bound structures using the Cα atoms. The value is reported for the loop in chain A for multimers.
d
RMSD obtained after superimposition of the loop region only.