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Structure of mouse H-chain modified ferritin

Analyse Structure of mouse H-chain modified ferritin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3WNW
Type
protein
Length
2,080 residues
Chains
12
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferritin heavy chain
EC
1.16.3.1
UniProt
P09528
Ligands
MG, FE, K
Pockets
20 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, H, I, KFerritin heavy chain (EC 1.16.3.1)protein17372% helix, 0% strandP09528
F, G, J, LFerritin heavy chain (EC 1.16.3.1)protein17472% helix, 0% strandP09528

Ligands and binding sites

  • MG · Magnesium ion · metal · 20 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
  • FE · Fe (III) ion · metal · 4 copies · chains A, J, B, F, C, E, I, K, H, L
  • K · Potassium ion · metal · 2 copies · chains B, C
  • GOL · Glycerol · additive · 12 copies · chains A, C, J, D, I, B, E, H, 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, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1770.760.9817empty
2530.730.9913empty
33160.670.8241MG
43080.660.8239MG
53180.660.8139MG

Interfaces

26 interfaces between chains.

  • H–K · 1621 Ų buried · 35 hydrogen bonds · protein-protein
  • D–I · 1611 Ų buried · 34 hydrogen bonds · protein-protein
  • C–J · 1606 Ų buried · 35 hydrogen bonds · protein-protein
  • B–E · 1598 Ų buried · 36 hydrogen bonds · protein-protein
  • G–I · 738 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 3WNW · Structure of Mouse H-chain modified ferritin · the same entry in another collection · chain L against L, TM-score 1.00

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