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. 2019 Jun 25;12(4):345–354. doi: 10.1007/s12195-019-00581-4

Table 1.

Occupancy rates of interactions between α4 and tubulin, the average distance between interacting atoms and the corresponding distance in the crystal structures.

Interactions between α4 and tubulin: occupancy rate (average distance) (distance in crystal structures)
Interacting residues Apo state ATP-binding state ADP-binding state
Leu248–Thr109 (α-tubulin) 100% (5.21 Å) (5.09 Å) 96.94% (6.53 Å) (7.48 Å) 0% (14.59 Å) (null)
Leu248–Tyr108 (α-tubulin) 100% (6.76 Å) (5.65 Å) 100% (5.12 Å) (6.55 Å) 6.37% (11.25Å) (null)
Leu248–Lys112 (α-tubulin) 99.75% (6.78 Å) (6.21 Å) 95.15% (7.17 Å) (4.88 Å) 32.32% (10.02 Å) (null)
Lys252–Glu411 (α-tubulin) 92.95% (6.04 Å) (4.99 Å) 99.98% (5.12 Å) (4.65 Å) 0% (16.15 Å) (null)
Asn255–Gly412 (α-tubulin) 98.94% (3.10 Å) (3.63 Å) 63.44% (3.85Å) (3.52 Å) 0% (12.39 Å) (null)
Ser259–Glu415 (α-tubulin) 26.40% (6.43 Å) (4.05 Å) 84.96% (3.93 Å) (5.29 Å) 12.27% (7.40 Å) (null)
Glu270–Lys401 (α-tubulin) 84.35% (6.72 Å) (8.20 Å) 95.53% (5.65 Å) (8.01 Å) 91.44% (5.62 Å) (null)
Asn263–Arg402 (α-tubulin) 63.73% (6.42 Å) (6.23 Å) 98.47% (4.92 Å) (6.13 Å) 26.57% (7.40 Å) (null)

Because there is no experimental structure of kineins-1 in ADP-binding state binds to tubulin, the distance of interacting atoms from experimental data is null. Crystal structures used: apo state-4LNU7 and ATP-binding state-4HNA14