2pu5

Crystal Structure of a C-C bond hydrolase, BphD, from Burkholderia xenovorans LB400Crystal Structure of a C-C bond hydrolase, BphD, from Burkholderia xenovorans LB400

Structural highlights

2pu5 is a 2 chain structure with sequence from Paraburkholderia xenovorans LB400. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BPHD_PARXL Catalyzes an unusual C-C bond hydrolysis of 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (HOPDA) to produce benzoic acid and 2-hydroxy-2,4-pentadienoic acid (HPD).^[1]

Evolutionary Conservation

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

References

↑ Horsman GP, Ke J, Dai S, Seah SY, Bolin JT, Eltis LD. Kinetic and structural insight into the mechanism of BphD, a C-C bond hydrolase from the biphenyl degradation pathway. Biochemistry. 2006 Sep 19;45(37):11071-86. PMID:16964968 doi:10.1021/bi0611098

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OCA

[1] Horsman GP, Ke J, Dai S, Seah SY, Bolin JT, Eltis LD. Kinetic and structural insight into the mechanism of BphD, a C-C bond hydrolase from the biphenyl degradation pathway. Biochemistry. 2006 Sep 19;45(37):11071-86. PMID:16964968 doi:10.1021/bi0611098

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