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Mbnabc complex

Analyse Mbnabc complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7DZ9
Type
protein
Length
925 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Mbnb; Cpmbnb; Mbnc; Mbna
UniProt
E3BK14, E3BK13
Ligands
FE
Pockets
6 · best druggability 0.85

Structure

x-ray diffraction · 5 distinct chains · 43% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMbnbprotein26045% helix, 20% strandE3BK14
BCpmbnbprotein26045% helix, 20% strandE3BK14
D, CMbncprotein18049% helix, 14% strandE3BK13
EMbnaprotein230% helix, 17% strand—
FMbnaprotein220% helix, 18% strand—

Ligands and binding sites

  • FE · Fe (III) ion · metal · 6 copies · chains A, F, B, E

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

Pockets

6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18140.850.8791empty
26470.840.8969empty
35820.840.8990empty
4860.710.9524empty
51210.630.8726empty

Interfaces

11 interfaces between chains.

  • B–C · 1645 Ų buried · 18 hydrogen bonds · protein-protein
  • A–D · 1618 Ų buried · 15 hydrogen bonds · protein-protein
  • D–F · 1052 Ų buried · 15 hydrogen bonds · protein-protein
  • E–C · 1010 Ų buried · 14 hydrogen bonds · protein-protein
  • B–E · 634 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 7DZ9 · MbnABC complex · the same entry in another collection · chain A against A, TM-score 1.00

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