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Heavy chain ferritin with C-terminal EBNA1 epitope

Analyse Heavy chain ferritin with C-terminal EBNA1 epitope in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7KE3
Type
protein
Length
2,001 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferritin heavy CHAIN,EPSTEIN-barr nuclear antigen 1
EC
1.16.3.1
UniProt
P02794
Ligands
FE
Pockets
20 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 75% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, DFerritin heavy CHAIN,EPSTEIN-barr nuclear antigen 1 (EC 1.16.3.1)protein16675% helix, 1% strandP02794
C, E, F, G, H, I, J, K, LFerritin heavy CHAIN,EPSTEIN-barr nuclear antigen 1 (EC 1.16.3.1)protein16775% helix, 1% strandP02794

Ligands and binding sites

  • FE · Fe (III) ion · metal · 20 copies · chains A, H, B, D, J, C, L, K, G, E, I, F
  • TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 6 copies · chains A, B, C, D, E, F, G, H, I, J, K, L

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

Pockets

20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1860.770.9816TRS
2840.750.9717TRS
3640.730.9814TRS
4570.720.9813TRS
5590.710.9714TRS

Interfaces

25 interfaces between chains.

  • A–B · 1551 Ų buried · 39 hydrogen bonds · protein-protein
  • I–J · 1548 Ų buried · 38 hydrogen bonds · protein-protein
  • E–F · 1544 Ų buried · 37 hydrogen bonds · protein-protein
  • K–L · 1541 Ų buried · 37 hydrogen bonds · protein-protein
  • G–H · 1531 Ų buried · 36 hydrogen bonds · protein-protein

Compared structures

  • 7KE3 · Heavy chain ferritin with C-terminal EBNA1 epitope · the same entry in another collection · chain L against L, TM-score 1.00

Analyse

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