9F6N: Human divalent metal transporter 1

Human divalent metal transporter 1 (DMT1/SLC11A2) in complex with manganese, in an occluded state. Determined by electron microscopy at 3.6 Å resolution. Released 27 Nov 2024.

Method: Electron microscopy
Resolution: 3.6 Å
Organism: Homo sapiens
Chains: 1
Atoms: 3,652
Mol. weight: 71.99 kDa
Ligands: MN
Released: 27 Nov 2024

Explore 9F6N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9F6N contains 23 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 23 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	96-101	6
α-helix	105-112	8
α-helix	116-128	13
α-helix	130-133	4
α-helix	135-157	23
α-helix	162-169	8
α-helix	172-204	33
α-helix	211-217	7
α-helix	220-231	12
α-helix	237-258	22
α-helix	262-270	9
α-helix	279-292	14
α-helix	297-307	11
α-helix	315-351	37
β-strand	355	1	1
α-helix	356-366	11
β-strand	380	1	1
α-helix	381	1
α-helix	385-429	45
α-helix	437-458	22
α-helix	461-478	18
α-helix	480-489	10
α-helix	493-496	4
α-helix	503-531	29
α-helix	536-561	26

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Natural resistance-associated macrophage protein 2	A	protein	655	Homo sapiens	P49281 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>9F6N_1 Natural resistance-associated macrophage protein 2 (chains A)
MSRKKQLKTEAAPHCELKSYSKNSATQVSTMVLGPEQKMSDDSVSGDHGESASLGNINPA
YSNPSLSQSPGDSEEYFATYFNEKISIPEEEYSCFSFRKLWAFTGPGFLMSIAYLDPGNI
ESDLQSGAVAGFKLLWILLLATLVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVPRVILW
LMVELAIIGSDMQEVIGSAIAINLLSVGRIPLWGGVLITIADTFVFLFLDKYGLRKLEAF
FGFLITIMALTFGYEYVTVKPSQSQVLKGMFVPSCSGCRTPQIEQAVGIVGAVIMPHNMY
LHSALVKSRQVNRNNKQEVREANKYFFIESCIALFVSFIINVFVVSVFAEAFFGKTNEQV
VEVCTNTSSPHAGLFPKDNSTLAVDIYKGGVVLGCYFGPAALYIWAVGILAAGQSSTMTG
TYSGQFVMEGFLNLKWSRFARVVLTRSIAIIPTLLVAVFQDVEHLTGMNDFLNVLQSLQL
PFALIPILTFTSLRPVMSDFANGLGWRIAGGILVLIICSINMYFVVVYVRDLGHVALYVV
AAVVSVAYLGFVFYLGWQCLIALGMSFLDCGHTVSISKGLLTEEATRGYVKALEVLFQGP
QGTEQKLISEEDLRGASMDEKTTGWRGGHVVEGLAGELEQLRARLEHHPQGQREP

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	1

Primary citation

Structural basis for metal ion transport by the human SLC11 proteins DMT1 and NRAMP1. Liziczai, M., Fuchs, A., Manatschal, C. et al. Nat Commun (2025) 16:761-761. DOI 10.1038/s41467-024-54705-0 · PubMed

Other PDB entries of the same protein (UniProt P49281 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5F0P 2.78 Å, Structure of retromer VPS26-VPS35 subunits bound to SNX3 and DMT1(L557M) (SeMet labeled)
5F0M 3.1 Å, Structure of retromer VPS26-VPS35 subunits bound to SNX3 and DMT1 (SeMet labeled)
5F0L 3.2 Å, Structure of retromer VPS26-VPS35 subunits bound to SNX3 and DMT1
9F6O 3.9 Å, Human divalent metal transporter 1 (DMT1/SLC11A2) in complex with sybody 1, in an…
7BLQ 9.2 Å, Vps26 dimer region of the fungal membrane-assembled retromer:Grd19 complex.
7BLO 9.5 Å, VPS26 dimer region of metazoan membrane-assembled retromer:SNX3 complex modelled with…

Browse structure collections

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