PDBsum entry 3ln6

Ligase

PDB id: 3ln6

Contents

Protein chain

743 a.a.

Ligands

SO4

Waters ×35

PDB id:

3ln6

Name:

Ligase

Title:

Crystal structure of a bifunctional glutathione synthetase from streptococcus agalactiae

Structure:

Glutathione biosynthesis bifunctional protein gshab. Chain: a. Synonym: gamma-gcs-gs, gcs-gs, glutamate-cysteine ligase, gamma- glutamylcysteine synthetase, gamma-ecs, gcs, glutathione synthetase, glutathione synthase, gsh synthetase, gsh-s, gshase, gs. Engineered: yes

Source:

Streptococcus agalactiae serogroup v. Organism_taxid: 216466. Strain: baa-811. Gene: gshab, gshf, sag1821. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.95Å R-factor: 0.253 R-free: 0.286

Authors:

J.Stout,B.Vergauwen,S.N.Savvides

Key ref:

J.Stout et al. Structures of two bifunctional gamma-Glutamate-Cystei ligase/glutathione synthetases (gshf) reveal a novel ATP-Grasp fold. To be published, .

Date:

02-Feb-10 Release date: 13-Apr-11

Protein chain

Q8DXM9  (GSHAB_STRA5) -  Glutathione biosynthesis bifunctional protein GshAB from Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)

Seq: 750 a.a.

Struc: 743 a.a.

Enzyme reactions

• Enzyme class 2: E.C.6.3.2.2 - glutamate--cysteine ligase.
• Reaction: L-cysteine + L-glutamate + ATP = gamma-L-glutamyl-L-cysteine + ADP + phosphate + H⁺
• Enzyme class 3: E.C.6.3.2.3 - glutathione synthase.
• Reaction: gamma-L-glutamyl-L-cysteine + glycine + ATP = glutathione + ADP + phosphate + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

Molecule diagrams generated from .mol files obtained from the KEGG ftp site