› 6prh

X-ray diffraction
2.08Å resolution

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128367 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uncharacterized protein YmcA Chain: A
Molecule details ›
Chain: A
Length: 124 amino acids
Theoretical weight: 14.18 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
  • Canonical: O31779 (Residues: 1-122; Coverage: 85%)
Gene names: BSU17020, ymcA
Sequence domains: Control of competence regulator ComK, YlbF/YmcA

Ligands and Environments

1 bound ligand:
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL14-1
Spacegroup: C2
Unit cell:
a: 109.491Å b: 52.212Å c: 27.109Å
α: 90° β: 95.83° γ: 90°
R-values:
R R work R free
0.185 0.183 0.224
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Bacillus subtilis biofilm formation and social interactions.
Arnaouteli et al. (2021)
10 other articles

1 mention without citation

Structure-Function Studies of the Bacillus subtilis Ric Proteins Identify the Fe-S Cluster-Ligating Residues and Their Roles in Development and RNA Processing.
Adusei-Danso et al. (2019)