3hq2

BsuCP Crystal StructureBsuCP Crystal Structure

Structural highlights

3hq2 is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.9Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CBP1_BACSU Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues. Has lower activity with substrates ending with His or Trp.^[1]

Evolutionary Conservation

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

References

↑ Lee MM, Isaza CE, White JD, Chen RP, Liang GF, He HT, Chan SI, Chan MK. Insight into the substrate length restriction of M32 carboxypeptidases: Characterization of two distinct subfamilies. Proteins. 2009 May 11;77(3):647-657. PMID:19544567 doi:10.1002/prot.22478

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OCA

[1] Lee MM, Isaza CE, White JD, Chen RP, Liang GF, He HT, Chan SI, Chan MK. Insight into the substrate length restriction of M32 carboxypeptidases: Characterization of two distinct subfamilies. Proteins. 2009 May 11;77(3):647-657. PMID:19544567 doi:10.1002/prot.22478

[1]

3hq2

BsuCP Crystal StructureBsuCP Crystal Structure

Structural highlights

Function

Evolutionary Conservation

See Also

References

Contents

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3hq2

BsuCP Crystal StructureBsuCP Crystal Structure

Structural highlights

Function

Evolutionary Conservation

See Also

References

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