Improvement of the Crystal Quality by the Surface Mutations on a Beta-Lactamase Toho-1
Shimamura, T., Nitanai, Y., Uchiyama, T., Ago, H., Matsuzawa, H., Miyano, M.To be published.
Experimental Data Snapshot
Starting Model: experimental
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wwPDB Validation   3D Report Full Report
Entity ID: 1 | |||||
---|---|---|---|---|---|
Molecule | Chains | Sequence Length | Organism | Details | Image |
Beta-lactamase Toho-1 | 262 | Escherichia coli | Mutation(s): 3  Gene Names: bla EC: 3.5.2.6 | ||
UniProt | |||||
Find proteins for Q47066 (Escherichia coli) Explore Q47066  Go to UniProtKB:  Q47066 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q47066 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 1 Unique | |||||
---|---|---|---|---|---|
ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
SO4 Query on SO4 | B [auth A], C [auth A], D [auth A], E [auth A], F [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |
Length ( ? ) | Angle ( ? ) |
---|---|
a = 72.545 | ¦Á = 90 |
b = 72.545 | ¦Â = 90 |
c = 97.656 | ¦Ă = 120 |
Software Name | Purpose |
---|---|
MOLREP | phasing |
REFMAC | refinement |
HKL-2000 | data collection |
HKL-2000 | data reduction |
SCALEPACK | data scaling |