The Structures of Aspartate Aminotransferase with Mutations of Non-Active-Site Residues
Tanaka, Y., Nakagawa, N., Tada, H., Yano, T., Masui, R., Kuramitsu, S.To be published.
Experimental Data Snapshot
Entity ID: 1 | |||||
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Molecule | Chains | Sequence Length | Organism | Details | Image |
Aspartate aminotransferase | 396 | Escherichia coli | Mutation(s): 14  Gene Names: aspC EC: 2.6.1.1 (PDB Primary Data), 2.6.1 (UniProt) | ||
UniProt | |||||
Find proteins for Q304P7 (Escherichia coli) Explore Q304P7  Go to UniProtKB:  Q304P7 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | Q304P7 | ||||
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 | C [auth A] | PYRIDOXAL-5'-PHOSPHATE C8 H10 N O6 P NGVDGCNFYWLIFO-UHFFFAOYSA-N | |||
SO4 Query on SO4 | B [auth A] | SULFATE ION O4 S QAOWNCQODCNURD-UHFFFAOYSA-L |
Length ( ? ) | Angle ( ? ) |
---|---|
a = 156.573 | ¦Á = 90 |
b = 85.274 | ¦Â = 90 |
c = 78.682 | ¦Ă = 90 |
Software Name | Purpose |
---|---|
CNS | refinement |
DENZO | data reduction |
SCALEPACK | data scaling |
AMoRE | phasing |