2dsk: 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=2dsk ConSurf].
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Revision as of 04:10, 9 February 2016

Crystal structure of catalytic domain of hyperthermophilic chitinase from Pyrococcus furiosusCrystal structure of catalytic domain of hyperthermophilic chitinase from Pyrococcus furiosus

Structural highlights

2dsk is a 2 chain structure with sequence from Atcc 43587. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Chitinase, with EC number 3.2.1.14
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Evolutionary Conservation

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

Publication Abstract from PubMed

The crystal structure of the catalytic domain of a chitinase from the hyperthermophilic archaeon Pyrococcus furiosus (AD2(PF-ChiA)) has been determined at 1.5 A resolution. This is the first structure of the catalytic domain of an archaeal chitinase. The overall structure of AD2(PF-ChiA) is a TIM-barrel fold with a tunnel-like active site that is a common feature of family 18 chitinases. Although the catalytic residues (Asp522, Asp524 and Glu526) are conserved, comparison of the conserved residues and structures with those of other homologous chitinases indicates that the catalytic mechanism of PF-ChiA is different from that of family 18 chitinases.

Structure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus.,Nakamura T, Mine S, Hagihara Y, Ishikawa K, Uegaki K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jan 1;63(Pt, 1):7-11. Epub 2006 Dec 16. PMID:17183162[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Nakamura T, Mine S, Hagihara Y, Ishikawa K, Uegaki K. Structure of the catalytic domain of the hyperthermophilic chitinase from Pyrococcus furiosus. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jan 1;63(Pt, 1):7-11. Epub 2006 Dec 16. PMID:17183162 doi:10.1107/S1744309106051773

2dsk, resolution 1.50Å

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OCA