1vqv

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Crystal Structure of Thiamine Monophosphate Kinase (thil) from Aquifex AeolicusCrystal Structure of Thiamine Monophosphate Kinase (thil) from Aquifex Aeolicus

Structural highlights

1vqv is a 2 chain structure with sequence from Aquifex aeolicus. This structure supersedes the now removed PDB entry 1yaw. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.65Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

THIL_AQUAE Catalyzes the ATP-dependent phosphorylation of thiamine-monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the active form of vitamin B1.[1]

Evolutionary Conservation

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

References

  1. McCulloch KM, Kinsland C, Begley TP, Ealick SE. Structural studies of thiamin monophosphate kinase in complex with substrates and products(,). Biochemistry. 2008 Mar 25;47(12):3810-21. Epub 2008 Mar 1. PMID:18311927 doi:10.1021/bi800041h

1vqv, resolution 2.65Å

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