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SEC13/SEC16 complex, S.CEREVISIAE

Analyse SEC13/SEC16 complex, S.CEREVISIAE in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3MZK
Type
protein
Length
1,360 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein transport protein SEC13; Protein transport protein SEC16
UniProt
Q04491, P48415
Pockets
19 · best druggability 0.87

Structure

x-ray diffraction · 3 distinct chains · 43% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, DProtein transport protein SEC13protein2973% helix, 56% strandQ04491
BProtein transport protein SEC16protein38559% helix, 4% strandP48415
CProtein transport protein SEC16protein38159% helix, 4% strandP48415

Pockets

19 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19430.870.8989empty
26910.870.9153empty
33380.650.8033empty
41280.630.8719empty
51780.630.8434empty

Interfaces

3 interfaces between chains.

  • B–C · 3059 Ų buried · 29 hydrogen bonds · protein-protein
  • C–D · 2913 Ų buried · 41 hydrogen bonds · protein-protein
  • A–B · 2903 Ų buried · 36 hydrogen bonds · protein-protein

Compared structures

  • 3MZK · Sec13/Sec16 complex, S.cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
  • P48415 · AlphaFold monomer V2.0 prediction for copii coat assembly protein SEC16 (P48415) · a predicted model of the same protein · chain C against A, TM-score 0.99
  • Q04491 · AlphaFold monomer V2.0 prediction for protein transport protein SEC13 (Q04491) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

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