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Cryoem structure of etec pilotin-secretin asps-gspd complex

Analyse Cryoem structure of etec pilotin-secretin asps-gspd complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5ZDH
Type
protein
Length
8,715 residues
Chains
30
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Type II secretion system protein D; Type II secretion system lipoprotein
UniProt
E3PJ86, E3PJ88
Pockets
20 · best druggability 0.81

Structure

electron microscopy · 2 distinct chains · 26% helix, 34% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, OType II secretion system protein Dprotein49725% helix, 36% strandE3PJ86
P, Q, R, S, T, U, V, W, X, Y, Z, a, b, c, dType II secretion system lipoproteinprotein8432% helix, 21% strandE3PJ88

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19770.810.83104empty
29470.810.8393empty
39730.810.8297empty
49450.810.8398empty
58930.810.83100empty

Interfaces

75 interfaces between chains.

  • E–F · 5691 Ų buried · 70 hydrogen bonds · protein-protein
  • M–N · 5688 Ų buried · 70 hydrogen bonds · protein-protein
  • A–O · 5684 Ų buried · 70 hydrogen bonds · protein-protein
  • H–I · 5679 Ų buried · 70 hydrogen bonds · protein-protein
  • K–L · 5678 Ų buried · 70 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 15 disulfide (disulfide).

Compared structures

  • 5ZDH · CryoEM structure of ETEC Pilotin-Secretin AspS-GspD complex · the same entry in another collection · chain K against K, TM-score 1.00

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