Trapping of the uric acid substrate in the crystal structure of urate oxidase from Arthrobacter globiformis
Juan, E.C.M., Hossain, M.T., Hoque, M.M., Yamamoto, T., Imamura, S., Suzuki, K., Sekiguchi, T., Takenaka, A.To be published.
Experimental Data Snapshot
Starting Model: experimental
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Entity ID: 1 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
Uricase | 302 | Arthrobacter globiformis | Mutation(s): 0 EC: 1.7.3.3 | ![]() | |
UniProt | |||||
Find proteins for D0VWQ1 (Arthrobacter globiformis) Explore D0VWQ1 Go to UniProtKB: D0VWQ1 | |||||
Entity Groups | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | D0VWQ1 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 1 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
AZA Query on AZA | I [auth A] J [auth B] K [auth C] L [auth D] M [auth E] | 8-AZAXANTHINE C4 H3 N5 O2 KVGVQTOQSNJTJI-UHFFFAOYSA-N |
Length ( Å ) | Angle ( ˚ ) |
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a = 83.33 | α = 90 |
b = 122.28 | β = 90 |
c = 283.92 | γ = 90 |
Software Name | Purpose |
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HKL-2000 | data collection |
AMoRE | phasing |
CNS | refinement |
HKL-2000 | data reduction |
HKL-2000 | data scaling |