MolNFT v1 · #168503 · protein

Cryo-EM structure of SLC40/FERROPORTIN with Fab in the presence of hepcidin

6WIK · 11F9 Fab light-chain: “Cryo-EM structure of SLC40/FERROPORTIN with Fab in the presence of hepcidin”. Electron microscopy, 16 pockets (best druggability 0.83). MolNFT v1 #168503 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 6WIK
Type: protein
Length: 859 residues
Chains: 3
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 11F9 Fab light-chain; 11F9 Fab heavy-chain; Solute carrier family 40 protein
UniProt: A0A1U7U6F1
Pockets: 16 · best druggability 0.83

Structure

electron microscopy · 3 distinct chains · 42% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
C	11F9 Fab light-chain	protein	213	4% helix, 42% strand	—
D	11F9 Fab heavy-chain	protein	219	5% helix, 46% strand	—
A	Solute carrier family 40 protein	protein	427	79% helix, 0% strand	A0A1U7U6F1

Pockets

16 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1110	0.83	0.84	85	empty
2	563	0.69	0.79	84	empty
3	344	0.66	0.80	41	empty
4	455	0.65	0.77	81	empty
5	317	0.63	0.80	43	empty

Interfaces

3 interfaces between chains.

C–D · 1198 Å² buried · 9 hydrogen bonds · protein-protein
D–A · 866 Å² buried · 10 hydrogen bonds · protein-protein
C–A · 349 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

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

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 A0A1U7U6F1
Elsewhere: RCSB PDB 6WIK · PDBe 6WIK · UniProt A0A1U7U6F1

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