1vqv: Difference between revisions

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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1vqv ConSurf].
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== References ==
== References ==

Revision as of 13:37, 7 February 2016

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"_huber_and_stetter_2001 "aquifex aeolicus" huber and stetter 2001. 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.
Ligands:
NonStd Res:
Activity:Thiamine-phosphate kinase, with EC number 2.7.4.16
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, 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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OCA
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