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Cryo-EM structure of SLC40/FERROPORTIN in complex with Fab

Analyse Cryo-EM structure of SLC40/FERROPORTIN in complex with Fab in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6VYH
Type
protein
Length
860 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Solute carrier family 40 protein; 11F9 light-chain; 11F9 heavy-chain
UniProt
A0A1U7U6F1
Ligands
CO
Pockets
14 · best druggability 0.84

Structure

electron microscopy · 3 distinct chains · 37% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASolute carrier family 40 proteinprotein42869% helix, 0% strandA0A1U7U6F1
C11F9 light-chainprotein2134% helix, 40% strand—
D11F9 heavy-chainprotein2195% helix, 46% strand—

Ligands and binding sites

  • CO · Cobalt (II) ion · metal · 2 copies · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110710.840.8596CO
25610.690.7984empty
34290.680.8065empty
42950.630.8032empty
52650.600.8043empty

Interfaces

3 interfaces between chains.

  • C–D · 1189 Ų buried · 9 hydrogen bonds · protein-protein
  • A–D · 857 Ų buried · 15 hydrogen bonds · protein-protein
  • A–C · 360 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 6VYH · Cryo-EM structure of SLC40/ferroportin in complex with Fab · the same entry in another collection · chain C against C, TM-score 1.00

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