GL1X · GenesisL1 explorer

Research workbench

Crystal structure of the minimal relaxase domain of moba from plasmid R1162

Analyse Crystal structure of the minimal relaxase domain of moba from plasmid R1162 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2NS6
Type
protein
Length
183 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mobilization protein a
EC
3.6.1.-
Ligands
MN

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMobilization protein a (EC 3.6.1.-)protein18336% helix, 21% strand—

Ligands and binding sites

  • MN · Manganese (II) ion · metal · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 2NS6 · Crystal Structure of the Minimal Relaxase Domain of MobA from Plasmid R1162 · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.