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MamM CTD E289D - Manganese form

Analyse MamM CTD E289D - Manganese form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6H9P
Type
protein
Length
252 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.1
Source
Magnetospirillum gryphiswaldense MSR-1
Molecule
Magnetosome protein MamM, Cation efflux protein family
UniProt
Q6NE57
Ligands
MN, SO4
Pockets
2 · best druggability 0.59

Structure

x-ray diffraction · resolution 2.1 · 3 distinct chains · 38% helix, 37% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMagnetosome protein MamM, Cation efflux protein familyprotein9235% helix, 34% strandQ6NE57
BMagnetosome protein MamM, Cation efflux protein familyprotein7939% helix, 39% strandQ6NE57
CMagnetosome protein MamM, Cation efflux protein familyprotein8140% helix, 37% strandQ6NE57

Ligands and binding sites

  • MN · Manganese (II) ion · metal · chains A
  • SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
  • BME · Beta-mercaptoethanol · additive · chains A

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

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11020.590.8716empty
2720.340.7614SO4

Interfaces

2 interfaces between chains.

  • B–C · 906 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 383 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

  • 6H9P · Mamm ctd E289D - manganese form · the same entry in another collection · chain A against A, TM-score 1.00

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