3mvn

X-ray diffraction
1.9Å resolution

Crystal structure of a domain from a putative UDP-N-acetylmuramate:L-alanyl-gamma-D-glutamyl-medo-diaminopimelate ligase from Haemophilus ducreyi 35000HP

Released:
Entry authors: Filippova EV, Minasov G, Shuvalova L, Kiryukhina O, Clancy S, Joachimiak A, Anderson FW, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-182070 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
UDP-N-acetylmuramate--L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptandioate ligase Chain: A
Molecule details ›
Chain: A
Length: 163 amino acids
Theoretical weight: 18.31 KDa
Source organism: [Haemophilus] ducreyi 35000HP
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q7VN73 (Residues: 315-453; Coverage: 30%)
Gene names: HD_0703, mpl
Sequence domains: Mur ligase, glutamate ligase domain
Structure domains: Mur ligase, C-terminal domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P41212
Unit cell:
a: 46.996Å b: 46.996Å c: 106.628Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.159 0.237
Expression system: Escherichia coli BL21