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Crystal structure of the human COPII-coat protein Sec24c

Analyse Crystal structure of the human COPII-coat protein Sec24c in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3EH2
Type
protein
Length
2,236 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.35
Source
Homo sapiens
Molecule
Protein transport protein Sec24C
UniProt
P53992
Ligands
ZN
Pockets
20 · best druggability 0.83

Structure

x-ray diffraction · resolution 2.35 · 3 distinct chains · 32% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein transport protein Sec24Cprotein75834% helix, 21% strandP53992
BProtein transport protein Sec24Cprotein73931% helix, 21% strandP53992
CProtein transport protein Sec24Cprotein73931% helix, 21% strandP53992

Ligands and binding sites

  • ZN · Zinc ion · metal · 3 copies · chains A, B, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18040.830.8587empty
26760.760.8156empty
35710.760.8363empty
41040.750.9623empty
55380.750.8257empty

Interfaces

3 interfaces between chains.

  • A–C · 1262 Ų buried · 17 hydrogen bonds · protein-protein
  • A–B · 1040 Ų buried · 24 hydrogen bonds · protein-protein
  • B–C · 76 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 3EH2 · Crystal structure of the human copii-coat protein SEC24C · the same entry in another collection · chain A against A, TM-score 1.00
  • P53992 · AlphaFold monomer V2.0 prediction for protein transport protein SEC24C (P53992) · a predicted model of the same protein · chain C against A, TM-score 0.99

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