GL1X · GenesisL1 explorer

MolNFT v1 · #77410 · protein

Copper (II) loaded bullfrog ferritin M chain

3RE7 · Ferritin, middle subunit: “Copper (II) loaded bullfrog ferritin M chain”. X-ray diffraction, 1 ligand (CU), 20 pockets (best druggability 0.81). MolNFT v1 #77410 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
3RE7
Type
protein
Length
4,128 residues
Chains
24
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferritin, middle subunit
EC
1.16.3.1
UniProt
P07798
Ligands
CU
Pockets
20 · best druggability 0.81

Structure

x-ray diffraction · 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, middle subunit (EC 1.16.3.1)protein17273% helix, 1% strandP07798

Ligands and binding sites

  • CU · Copper (II) ion · metal · 162 copies · chains A, J, O, R, G, X, B, H, I, E, V, C, S, D, K, Q, W, L, P, F, M, N, U, T

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
11590.810.9727empty
21420.810.9725empty
31460.800.9727empty
41400.800.9730empty
51190.800.9823empty

Interfaces

72 interfaces between chains.

  • M–S · 1606 Ų buried · 28 hydrogen bonds · protein-protein
  • A–G · 1588 Ų buried · 36 hydrogen bonds · protein-protein
  • N–R · 1588 Ų buried · 34 hydrogen bonds · protein-protein
  • E–I · 1587 Ų buried · 29 hydrogen bonds · protein-protein
  • L–V · 1587 Ų buried · 28 hydrogen bonds · protein-protein

Compared structures

  • 3RE7 · Copper (II) loaded Bullfrog Ferritin M chain · the same entry in another collection · chain J against J, TM-score 1.00

Analyse

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