Transition state of phospho-enzyme hydrolysis in beta-phosphoglucomutase.
Robertson, A.J., Bisson, C., Waltho, J.P.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 |
Beta-phosphoglucomutase | 221 | Lactococcus lactis subsp. lactis Il1403 | Mutation(s): 3  Gene Names: pgmB, LL0429, L0001 EC: 5.4.2.6 | ||
UniProt | |||||
Find proteins for P71447 (Lactococcus lactis subsp. lactis (strain IL1403)) Explore P71447  Go to UniProtKB:  P71447 | |||||
Entity Groups   | |||||
Sequence Clusters | 30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity | ||||
UniProt Group | P71447 | ||||
Sequence AnnotationsExpand | |||||
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Ligands 2 Unique | |||||
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ID | Chains | Name / Formula / InChI Key | 2D Diagram | 3D Interactions | |
EDO Query on EDO | D [auth A], E [auth A], F [auth A], H [auth B] | 1,2-ETHANEDIOL C2 H6 O2 LYCAIKOWRPUZTN-UHFFFAOYSA-N | |||
MG Query on MG | C [auth A], G [auth B] | MAGNESIUM ION Mg JLVVSXFLKOJNIY-UHFFFAOYSA-N |
Length ( ? ) | Angle ( ? ) |
---|---|
a = 38.2 | ¦Á = 90 |
b = 116.9 | ¦Â = 98.09 |
c = 53.17 | ¦Ă = 90 |
Software Name | Purpose |
---|---|
REFMAC | refinement |
xia2 | data reduction |
xia2 | data scaling |
MOLREP | phasing |
Funding Organization | Location | Grant Number |
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Biotechnology and Biological Sciences Research Council | United Kingdom | BB/M021637/1 |
Biotechnology and Biological Sciences Research Council | United Kingdom | BB/K016245/1 |