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Cryo-electron microscopy structure of the heavy metal efflux pump cusa in a heterogeneous 2 open and 1 closed protomer conformation

Analyse Cryo-electron microscopy structure of the heavy metal efflux pump cusa in a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7KF8
Type
protein
Length
3,055 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cation efflux system protein cusa
UniProt
P38054
Ligands
CU1
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 2 distinct chains · 52% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACation efflux system protein cusaprotein102552% helix, 17% strandP38054
B, CCation efflux system protein cusaprotein101552% helix, 17% strandP38054

Ligands and binding sites

  • CU1 · Copper (I) ion · metal · 2 copies · chains B, C

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
110820.840.8592empty
210280.830.8494empty
38650.830.8593empty
48730.800.83102empty
56990.770.8273empty

Interfaces

3 interfaces between chains.

  • B–C · 3304 Ų buried · 26 hydrogen bonds · protein-protein
  • A–C · 3003 Ų buried · 27 hydrogen bonds · protein-protein
  • A–B · 2913 Ų buried · 24 hydrogen bonds · protein-protein

Compared structures

  • 7KF8 · Cryo-electron microscopy structure of the heavy metal efflux pump CusA in a heterogeneous… · the same entry in another collection · chain A against A, TM-score 1.00
  • P38054 · AlphaFold monomer V2.0 prediction for cation efflux system protein cusa (P38054) · a predicted model of the same protein · chain A against A, TM-score 0.98

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