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MolNFT v1 · #156465 · protein

Human apo ferritin frozen on tem grid with amorphous nickel titanium alloy supporting film

6M54 · Ferritin heavy chain: “Human apo ferritin frozen on tem grid with amorphous nickel titanium alloy supporting film”. Electron microscopy, 1 ligand (FE2), 20 pockets (best druggability 0.75). MolNFT v1 #156465 on GenesisL1: 3D…

PDB
6M54
Type
protein
Length
4,104 residues
Chains
24
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferritin heavy chain
EC
1.16.3.1
UniProt
P02794
Ligands
FE2
Pockets
20 · best druggability 0.75

Structure

electron microscopy · 1 distinct chain · 73% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W, XFerritin heavy chain (EC 1.16.3.1)protein17173% helix, 1% strandP02794

Ligands and binding sites

  • FE2 · Fe (II) ion · metal · 6 copies · chains A, D, Q, T, B, C, R, S, E, H, M, P, F, G, N, O, I, L, V, W, J, K, U, X

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1710.750.9812empty
2750.740.9713empty
3740.730.9713empty
4760.730.9713empty
5740.730.9714empty

Interfaces

71 interfaces between chains.

  • A–V · 1520 Ų buried · 14 hydrogen bonds · protein-protein
  • H–R · 1519 Ų buried · 12 hydrogen bonds · protein-protein
  • I–P · 1519 Ų buried · 13 hydrogen bonds · protein-protein
  • B–W · 1518 Ų buried · 12 hydrogen bonds · protein-protein
  • D–U · 1517 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 6M54 · Human apo ferritin frozen on TEM grid with Amorphous nickel titanium alloy supporting film · the same entry in another collection · chain K against K, TM-score 1.00

Analyse

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