Structure-based mutation analysis GLA

^{by Benjamin Drexler and Fabian Grandke}

Introduction

In this task we analyse the structure of our protein to find out what effects the point mutations have. Therefor we create a mutated structure and compare it to the wild-type protein.

Structure Selection

There are several structure files available for our protein:

PDB ID	Resolution [Å]	ph-Value	R-Factor	Coverage [%]	Missing Residues
1R46	3.25	8.0	0.262	99.7	422-429
1R47	3.45	8.0	0.285	99.5	422-429
3GXN	3.01	NULL	0.239	88.08	422-429
3GXP	2.20	NULL	0.204	81.9	422-429
3GXT	2.70	NULL	0.245	97.29	422-429
3HG2	2.30	4.6	0.178	97.32	422-429
3HG3	1.90	6.5	0.167	98.64	427-435
3HG4	2.30	4.6	0.166	99.86	422-429
3HG5	2.30	4.6	0.192	100	422-429
3LX9	2.04	6.5	0.178	98.92	423-435
3LXA	3.04	6.5	0.216	99.52	427-435
3LXB	2.85	6.5	0.227	99.3	427-435
3LXC	2.35	6.5	0.186	98.31	423-435

We set two cutoffs to decide which structures are excluded:

• ph-value: < 6.5
• resolution: > 2.7

After we applied the cutoffs to our set of structures three were left (exclusion factors are colored red in the table). One of them was slightly better than the other ones so we decided to use 3HG3 (worse values are colored gray in the table). Additionally 3GH3 has the best resolution and R-factor (colored green). As the missing residues are very similar for all structures they are not further taken into account.

References

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