2fff

X-ray diffraction
2.23Å resolution

Open Form of a Class A Transpeptidase Domain

Released:

Function and Biology Details

Reaction catalysed:
(GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n)-diphosphoundecaprenol + GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-diphosphoundecaprenol = (GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala))(n+1)-diphosphoundecaprenol + undecaprenyl diphosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-130674 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
peptidoglycan glycosyltransferase Chain: A
Molecule details ›
Chain: A
Length: 15 amino acids
Theoretical weight: 1.57 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q4TUQ1 (Residues: 74-88; Coverage: 2%)
Gene name: pbp1b
peptidoglycan glycosyltransferase Chain: B
Molecule details ›
Chain: B
Length: 453 amino acids
Theoretical weight: 49.87 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O70038 (Residues: 337-789; Coverage: 55%)
Gene name: pbp1b
Sequence domains: Penicillin binding protein transpeptidase domain
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 131.661Å b: 78.043Å c: 60.315Å
α: 90° β: 113.02° γ: 90°
R-values:
R R work R free
0.186 0.183 0.246
Expression system: Escherichia coli BL21