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Cryo-EM structure of the mamk filament at 6.5 a

Analyse Cryo-EM structure of the mamk filament at 6.5 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5JYG
Type
protein
Length
4,592 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Actin-like ATPase
UniProt
Q2W8Q6
Ligands
ADP, MG
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 34% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, NActin-like ATPaseprotein32834% helix, 20% strandQ2W8Q6

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 14 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N
  • MG · Magnesium ion · metal · 14 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19110.860.88113MG, ADP
210440.850.85101MG, ADP
310570.840.85112MG, ADP
412000.840.85127MG, ADP
511030.830.84114MG, ADP

Interfaces

19 interfaces between chains.

  • A–H · 716 Ų buried · 5 hydrogen bonds · protein-protein
  • D–E · 691 Ų buried · 6 hydrogen bonds · protein-protein
  • I–J · 690 Ų buried · 6 hydrogen bonds · protein-protein
  • G–N · 689 Ų buried · 6 hydrogen bonds · protein-protein
  • M–N · 689 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 5JYG · Cryo-EM structure of the MamK filament at 6.5 A · the same entry in another collection · chain N against N, TM-score 1.00

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