PDBsum entry 5glb

Hydrolase

PDB id

5glb

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Contents

			Protein chain

					268 a.a.

			Ligands

					CB4

			Waters ×255

PDB id:

5glb

Links

Name:

Hydrolase

Title:

Crystal structure of the class a beta-lactamase penl-ttr10 in complex with cba

Structure:

Beta-lactamase. Chain: a. Fragment: unp residues 31-294. Engineered: yes

Source:

Burkholderia thailandensis. Organism_taxid: 57975. Gene: a8h35_31635. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

Resolution:

1.60Å

R-factor:

0.163

R-free:

0.200

Authors:

J.M.Choi,H.Yi,H.S.Kim,S.H.Lee

Key ref:

H.Yi et al. (2016). High adaptability of the omega loop underlies the substrate-spectrum-extension evolution of a class A β-lactamase, PenL. Sci Rep, 6, 36527. PubMed id: 27827433 DOI: 10.1038/srep36527

Date:

10-Jul-16

Release date:

15-Feb-17

PROCHECK

	Headers

	References

Protein chain

Q2T5A3 (Q2T5A3_BURTA) - Beta-lactamase from Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CCUG 48851 / CIP 106301 / E264)

Seq: Struc:					322 a.a. 268 a.a.*

Key:

PfamA domain

Secondary structure

CATH domain

* PDB and UniProt seqs differ at 4 residue positions (black crosses)



		Enzyme reactions

Enzyme class:

E.C.3.5.2.6 - beta-lactamase.

[IntEnz] [ExPASy] [KEGG] [BRENDA]

Pathway:

Penicillin Biosynthesis and Metabolism

Reaction:

a beta-lactam + H2O = a substituted beta-amino acid

Cofactor:

Zn(2+)

DOI no: 10.1038/srep36527	Sci Rep 6:36527 (2016)
PubMed id: 27827433

High adaptability of the omega loop underlies the substrate-spectrum-extension evolution of a class A β-lactamase, PenL.
H.Yi, J.M.Choi, J.Hwang, F.Prati, T.P.Cao, S.H.Lee, H.S.Kim.

ABSTRACT

No abstract given.