GL1X · GenesisL1 explorer

MolNFT v1 · #156065 · protein

Rod-shaped crystal of tmftn mutant-T4FY stimulited by PLL15

6LS0 · Ferritin: “Rod-shaped crystal of tmftn mutant-T4FY stimulited by PLL15”. X-ray diffraction, 1 ligand (FE), 5 pockets (best druggability 0.71). MolNFT v1 #156065 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6LS0
Type
protein
Length
651 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ferritin
EC
1.16.3.2
UniProt
Q9X0L2
Ligands
FE
Pockets
5 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 78% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
H, A, BFerritin (EC 1.16.3.2)protein16377% helix, 1% strandQ9X0L2
CFerritin (EC 1.16.3.2)protein16279% helix, 0% strandQ9X0L2

Ligands and binding sites

  • FE · Fe (III) ion · metal · 7 copies · chains H, A, B, C

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

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18560.710.7665empty
22590.710.8527empty
31250.420.7620empty
4660.310.7413empty
5530.290.7516empty

Interfaces

4 interfaces between chains.

  • H–B · 1283 Ų buried · 24 hydrogen bonds · protein-protein
  • H–A · 518 Ų buried · 7 hydrogen bonds · protein-protein
  • A–C · 517 Ų buried · 6 hydrogen bonds · protein-protein
  • B–C · 390 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 6LS0 · rod-shaped crystal of TmFtn mutant-T4FY stimulited by PLL15 · the same entry in another collection · chain H against H, TM-score 1.00

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