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Cryoem structure of the outer membrane secretin pore piv from the F1 filamentous bacteriophage.

Analyse Cryoem structure of the outer membrane secretin pore piv from the F1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7OFH
Type
protein
Length
3,465 residues
Chains
15
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Virion export protein
UniProt
P03666
Ligands
CPS
Pockets
20 · best druggability 0.69

Structure

electron microscopy · 1 distinct chain · 6% helix, 58% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, OVirion export proteinprotein2316% helix, 58% strandP03666

Ligands and binding sites

  • CPS · 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate · ligand · 30 copies · chains A, O, 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
16860.690.7790empty
26970.690.7783empty
34820.650.7758empty
44630.640.7762empty
54280.630.7755empty

Interfaces

15 interfaces between chains.

  • A–O · 2599 Ų buried · 42 hydrogen bonds · protein-protein
  • G–H · 2596 Ų buried · 42 hydrogen bonds · protein-protein
  • N–O · 2595 Ų buried · 42 hydrogen bonds · protein-protein
  • F–G · 2594 Ų buried · 41 hydrogen bonds · protein-protein
  • B–C · 2594 Ų buried · 42 hydrogen bonds · protein-protein

Compared structures

  • 7OFH · CryoEM structure of the outer membrane secretin pore pIV from the f1 filamentous… · the same entry in another collection · chain A against A, TM-score 1.00

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