Table 2.
Residues Located at Kinks in Transmembrane α-Helices
| Membraneprotein | Transmembranehelix | Residuesat kink |
|---|---|---|
| Bacteriorhodopsin (1AP9) | A | L22, G23 |
| B | V49, P50 | |
| G | K216, V217, G218 | |
| Cytochrome c oxidase (1OCC) | I (I) | A26, G27 |
| II (I) | G76 | |
| II (I) | M69, V70 | |
| V (I) | S198, L199 | |
| VI (I) | L248, P249 | |
| X (I) | L381, S382 | |
| XI (I) | P427, Q428 | |
| II (II) | I67, L68, P69 | |
| II (II) | L78, P79 | |
| I (VIc) | V39, A40, E41 | |
| I (VIII) | F26, L27 | |
| I (VIII) | L37 | |
| Calcium pump (1EUL) | M3 | S261 |
| M4 | K297, I298 | |
| M6 | G801, L802 | |
| M10 | S974, L975, P976 | |
| Halorhodopsin (1E12) | A | S32, L33 |
| C | S115 | |
| E | T181, D182 | |
| G | K242, Y243 | |
| F | W207, L208, G209 | |
| Photosynthetic | A (L) | G45, V46 |
| reaction center (1PRC) | C (L) | C122, V123, P124 |
| C (L) | V133, F134 | |
| E (L) | T241, L242 | |
| C (M) | G159, C160 | |
| E (M) | F269, F270, S271 | |
| Rhodopsin (1F88) | I | G51, F52, P53 |
| II | G89, G90 | |
| III | G120 | |
| V | F212, I213 | |
| VI | C264, W265 | |
| VII | S298, A299, V300 |
The first column gives the membrane protein name with PDB accession code indicated in parentheses. The transmembrane helices that have kinks are shown in the second column where for heteromultimeric proteins (Cytochrome c oxidase and Photosynthetic reaction center) the letters in parentheses indicate the subunit to which the helix belongs. The third column indicates the position and identity of residues found at kinks, with one line for each kink. Pro, Gly, and Ser residues are shown in bold.