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Structure of post-translational translocation SEC71/SEC72 complex

Analyse Structure of post-translational translocation SEC71/SEC72 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5L0W
Type
protein
Length
371 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
SEC72; SEC71
UniProt
G0SH41, G0S0B5
Pockets
2 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 68% helix, 2% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
BSEC72protein20965% helix, 3% strandG0SH41
ASEC71protein16272% helix, 0% strandG0S0B5

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11370.400.7424empty
2870.360.7520empty

Interfaces

1 interface between chains.

  • B–A · 2316 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 modified (engineered).

Compared structures

  • 5L0W · Structure of post-translational translocation Sec71/Sec72 complex · the same entry in another collection · chain B against B, TM-score 1.00

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