8bv4

Structure of BlaC from Mycobacterium tuberculosis in complex with vaborbactamStructure of BlaC from Mycobacterium tuberculosis in complex with vaborbactam

Structural highlights

8bv4 is a 1 chain structure with sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.95Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BLAC_MYCTA Extended spectrum beta-lactamase (ESBL) that inactivates beta-lactam antibiotics by hydrolyzing the amide group of the beta-lactam ring. Exhibits predominant penicillinase activity. Also displays high levels of cephalosporinase activity as well as measurable activity with carbapenems, including imipenem and meropenem. Plays a primary role in the intrinsic resistance of M.tuberculosis to beta-lactam antibiotics.[UniProtKB:P9WKD3]^[1]

References

↑ Voladri RK, Lakey DL, Hennigan SH, Menzies BE, Edwards KM, Kernodle DS. Recombinant expression and characterization of the major beta-lactamase of Mycobacterium tuberculosis. Antimicrob Agents Chemother. 1998 Jun;42(6):1375-81. PMID:9624479 doi:10.1128/AAC.42.6.1375

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OCA

[1] Voladri RK, Lakey DL, Hennigan SH, Menzies BE, Edwards KM, Kernodle DS. Recombinant expression and characterization of the major beta-lactamase of Mycobacterium tuberculosis. Antimicrob Agents Chemother. 1998 Jun;42(6):1375-81. PMID:9624479 doi:10.1128/AAC.42.6.1375

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