X-Ray studies on protein complexes: Enzymatic catalysis in Crystals of E.coli Maltodextrin Phosphorylase (MalP)
Geremia, S., Campagnolo, M.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 |
Maltodextrin phosphorylase | 796 | Escherichia coli | Mutation(s): 3  Gene Names: EG10560 EC: 2.4.1.1 | ||
UniProt | |||||
Find proteins for P00490 (Escherichia coli (strain K12)) Explore P00490  Go to UniProtKB:  P00490 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P00490 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 3 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
PLP Query on PLP | G [auth A], J [auth B] | PYRIDOXAL-5'-PHOSPHATE C8 H10 N O6 P NGVDGCNFYWLIFO-UHFFFAOYSA-N | |||
ASO Query on ASO | E [auth A], H [auth B] | 1,5-anhydro-D-glucitol C6 H12 O5 MPCAJMNYNOGXPB-SLPGGIOYSA-N | |||
PO4 Query on PO4 | F [auth A], I [auth B] | PHOSPHATE ION O4 P NBIIXXVUZAFLBC-UHFFFAOYSA-K |
Length ( Å ) | Angle ( ˚ ) |
---|---|
a = 74.327 | α = 90 |
b = 104.723 | β = 90 |
c = 214.787 | γ = 90 |
Software Name | Purpose |
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REFMAC | refinement |
MAR345 | data collection |
CCP4 | data scaling |