Mechanism of broad substrate specificity of alpha-aminoadipate aminotransferase from Thermus thermophilus
Tomita, T., Miyazaki, T., Miyagawa, T., Fushinobu, S., Kuzuyama, T., Nishiyama, M.To be published.
Experimental Data Snapshot
Starting Model: experimental
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wwPDB Validation   3D Report Full Report
Entity ID: 1 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
Alpha-aminodipate aminotransferase | 397 | Thermus thermophilus | Mutation(s): 0  Gene Names: lysN EC: 2.6.1.39 | ||
UniProt | |||||
Find proteins for Q72LL6 (Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)) Explore Q72LL6  Go to UniProtKB:  Q72LL6 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q72LL6 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 2 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
PLP Query on PLP | D [auth A], F [auth B] | PYRIDOXAL-5'-PHOSPHATE C8 H10 N O6 P NGVDGCNFYWLIFO-UHFFFAOYSA-N | |||
LEU Query on LEU | C [auth A], E [auth B] | LEUCINE C6 H13 N O2 ROHFNLRQFUQHCH-YFKPBYRVSA-N |
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 137.107 | α = 90 |
b = 62.229 | β = 116.34 |
c = 107.439 | γ = 90 |
Software Name | Purpose |
---|---|
CNS | refinement |
HKL-2000 | data collection |
HKL-2000 | data reduction |
HKL-2000 | data scaling |
MOLREP | phasing |