Table 2.
Conservation of hydrogen bonding interactions of Asn43 in PYP and other PAS domains.
| Helical cap helix 3 |
Link to β-strand 1 |
||||
|---|---|---|---|---|---|
| Proteina (PBD) | Residueb | lengthc | lengthc | ||
| Hh PYP (1NWZ) | Asn43 | Glu46 | 2.9 | Ala30 | 2.9 |
| Rm FixL (1D06) | Asn163 | Ala166 | 2.8 | Thr150 | 2.8 |
| Av NifL (2GJ3) | Asn51 | Phe54 | 2.9 | Ile38 | 3.0 |
| Ec DOS – O2 (1VB6) | Asn46 | Ala49 | 2.9 | Ala33 | 2.8 |
| Ec DOS + O2 (1S67) | Asn46 | H2O | 2.6 | - | |
| Hs ERG (1BYW) | Asn45 | Phe48 | 2.9 | Phe29 | 3.2 |
| Hs PasK (lLL8) | Asn25 | Ala28 | 3.2 | Ile11 | 3.4 |
| Bs YtvA (2PR5) | Asn43 | Phe46 | 2.9 | Val27 | 2.9 |
| Bj FixL (1DP6) | Ser169 | Ala172 | 3.4 | Met156 | 3.2 |
| Ac LOV2 (1G28) | Ser947 | Phe950 | 3.3 | Phe931 | 3.0 |
| Cr LOV1 (1N9L) | Ser38 | Phe41 | 3.2 | Phe22 | 3.1 |
a
Hh = Halorhodospira halophila; Rm = Rhizobium meliloti; Av = Azotobacter vinelandii; Ec = Escherichia coli; Hs = Homo sapiens; Bs = Bacillus subtilis; Bj = Bradyrhizobium japonicum; Ac =Adantium capillus-veneris; Cr = Chlamydomonas reinhardtii.
b
Hydrogen bond from the side chain of Asn43 and corresponding residues to the backbone NH group of the indicated residue.
c
Hydrogen bonding length is indicated in Å.