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Structure of apo human ferroportin in lipid nanodisc

Analyse Structure of apo human ferroportin in lipid nanodisc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6W4S
Type: protein
Length: 650 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Solute carrier family 40 member 1; FAB45D8 heavy chain; FAB45D8 light chain
UniProt: Q9NP59
Pockets: 2 · best druggability 0.83

Structure

electron microscopy · 3 distinct chains · 55% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
F	Solute carrier family 40 member 1	protein	421	85% helix, 0% strand	Q9NP59
H	FAB45D8 heavy chain	protein	118	0% helix, 54% strand	—
L	FAB45D8 light chain	protein	111	0% helix, 44% strand	—

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	867	0.83	0.85	80	empty
2	58	0.28	0.74	13	empty

Interfaces

3 interfaces between chains.

H–L · 901 Å² buried · 7 hydrogen bonds · protein-protein
F–L · 374 Å² buried · 10 hydrogen bonds · protein-protein
F–H · 303 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

6W4S · Structure of apo human ferroportin in lipid nanodisc · the same entry in another collection · chain F against F, TM-score 1.00
Q9NP59 · AlphaFold monomer V2.0 prediction for solute carrier family 40 member 1 (Q9NP59) · a predicted model of the same protein · chain F against A, TM-score 0.96

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9NP59
Elsewhere: RCSB PDB 6W4S · PDBe 6W4S · UniProt Q9NP59

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