2ith

NMR Structure of Haloferax volcanii DHFRNMR Structure of Haloferax volcanii DHFR

Structural highlights

2ith is a 1 chain structure with sequence from Haloferax volcanii. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DYRA_HALVD Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Zusman T, Rosenshine I, Boehm G, Jaenicke R, Leskiw B, Mevarech M. Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii. The enzyme and its coding gene. J Biol Chem. 1989 Nov 15;264(32):18878-83 PMID:2509470

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OCA

[1] Zusman T, Rosenshine I, Boehm G, Jaenicke R, Leskiw B, Mevarech M. Dihydrofolate reductase of the extremely halophilic archaebacterium Halobacterium volcanii. The enzyme and its coding gene. J Biol Chem. 1989 Nov 15;264(32):18878-83 PMID:2509470

[1]

2ith

NMR Structure of Haloferax volcanii DHFRNMR Structure of Haloferax volcanii DHFR

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

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2ith

NMR Structure of Haloferax volcanii DHFRNMR Structure of Haloferax volcanii DHFR

Structural highlights

Function

Evolutionary Conservation

See Also

References

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