1nl3

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF THE SECA PROTEIN TRANSLOCATION ATPASE FROM MYCOBACTERIUM TUBERCULOSIS in APO FORM

Released:

Function and Biology Details

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein translocase subunit SecA 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 922 amino acids
Theoretical weight: 103.46 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WGP5 (Residues: 2-892; Coverage: 94%)
Gene names: MTCY20B11.15c, Rv3240c, secA1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P6222
Unit cell:
a: 206.196Å b: 206.196Å c: 295.412Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.196 0.193 0.259
Expression system: Escherichia coli BL21(DE3)