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Cryo-EM structure of yiip-Fab complex in apo state

Analyse Cryo-EM structure of yiip-Fab complex in apo state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7KZX
Type
protein
Length
1,361 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cadmium and zinc efflux pump fief; FAB2R light chain; FAB2R heavy chain
UniProt
Q8E919
Pockets
17 · best druggability 0.83

Structure

electron microscopy · 4 distinct chains · 24% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCadmium and zinc efflux pump fiefprotein28163% helix, 10% strandQ8E919
CFAB2R light chainprotein1906% helix, 40% strand—
D, FFAB2R heavy chainprotein2094% helix, 45% strand—
EFAB2R light chainprotein1916% helix, 43% strand—

Pockets

17 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18140.830.8582empty
22720.700.8439empty
31330.610.8532empty
42540.610.8022empty
54190.570.7451empty

Interfaces

7 interfaces between chains.

  • A–B · 2674 Ų buried · 22 hydrogen bonds · protein-protein
  • E–F · 1932 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 1926 Ų buried · 7 hydrogen bonds · protein-protein
  • A–F · 785 Ų buried · 6 hydrogen bonds · protein-protein
  • B–D · 729 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

  • 7KZX · Cryo-EM structure of YiiP-Fab complex in Apo state · the same entry in another collection · chain A against A, TM-score 1.00

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