Human divalent metal transporter 1 (DMT1/SLC11A2) in complex with sybody 1, in an occluded state. Determined by electron microscopy at 3.9 Å resolution. Released 27 Nov 2024.
Explore 9F6O in 3D Show helices and sheets RCSB PDB PDBe
9F6O contains 26 α-helices and 11 β-strands across 2 chains. 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 96-101 | 6 | |
| α-helix | 105-111 | 7 | |
| α-helix | 116-127 | 12 | |
| α-helix | 132-134 | 3 | |
| α-helix | 135-157 | 23 | |
| α-helix | 162-167 | 6 | |
| α-helix | 172-204 | 33 | |
| α-helix | 211-217 | 7 | |
| α-helix | 219-231 | 13 | |
| α-helix | 237-258 | 22 | |
| α-helix | 262-270 | 9 | |
| α-helix | 279-292 | 14 | |
| α-helix | 297-307 | 11 | |
| α-helix | 315-350 | 36 | |
| α-helix | 356-366 | 11 | |
| α-helix | 385-429 | 45 | |
| α-helix | 437-458 | 22 | |
| α-helix | 461-477 | 17 | |
| α-helix | 480-482 | 3 | |
| α-helix | 484-489 | 6 | |
| α-helix | 493-496 | 4 | |
| α-helix | 500-502 | 3 | |
| α-helix | 503-531 | 29 | |
| α-helix | 536-561 | 26 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-7 | 5 | 1 |
| β-strand | 10-12 | 3 | 2 |
| β-strand | 17-25 | 9 | 1 |
| α-helix | 29-31 | 3 | |
| β-strand | 34-39 | 6 | 2 |
| β-strand | 46-51 | 6 | 2 |
| β-strand | 59-60 | 2 | 2 |
| β-strand | 68-73 | 6 | 1 |
| β-strand | 78-84 | 7 | 1 |
| α-helix | 88-90 | 3 | |
| β-strand | 92-100 | 9 | 2 |
| β-strand | 108-110 | 3 | 2 |
| β-strand | 115-119 | 5 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Natural resistance-associated macrophage protein 2 | A | protein | 655 | Homo sapiens | P49281 (AlphaFold model) |
| Sybody 1 | B | protein | 146 | synthetic construct |
>9F6O_1 Natural resistance-associated macrophage protein 2 (chains A) MSRKKQLKTEAAPHCELKSYSKNSATQVSTMVLGPEQKMSDDSVSGDHGESASLGNINPA YSNPSLSQSPGDSEEYFATYFNEKISIPEEEYSCFSFRKLWAFTGPGFLMSIAYLDPGNI ESDLQSGAVAGFKLLWILLLATLVGLLLQRLAARLGVVTGLHLAEVCHRQYPKVPRVILW LMVELAIIGSDMQEVIGSAIAINLLSVGRIPLWGGVLITIADTFVFLFLDKYGLRKLEAF FGFLITIMALTFGYEYVTVKPSQSQVLKGMFVPSCSGCRTPQIEQAVGIVGAVIMPHNMY LHSALVKSRQVNRNNKQEVREANKYFFIESCIALFVSFIINVFVVSVFAEAFFGKTNEQV VEVCTNTSSPHAGLFPKDNSTLAVDIYKGGVVLGCYFGPAALYIWAVGILAAGQSSTMTG TYSGQFVMEGFLNLKWSRFARVVLTRSIAIIPTLLVAVFQDVEHLTGMNDFLNVLQSLQL PFALIPILTFTSLRPVMSDFANGLGWRIAGGILVLIICSINMYFVVVYVRDLGHVALYVV AAVVSVAYLGFVFYLGWQCLIALGMSFLDCGHTVSISKGLLTEEATRGYVKALEVLFQGP QGTEQKLISEEDLRGASMDEKTTGWRGGHVVEGLAGELEQLRARLEHHPQGQREP
>9F6O_2 Sybody 1 (chains B) QVQLVESGGGLVQAGGSLRLSCAASGFPVSRSEMYWYRQAPGKEREWVAAIHSIGWNTRY ADSVKGRFTISRDNAKNTVYLQMNSLKPEDTAVYYCNVKDAGWFWTNYDYWGQGTQVTVS AGRAGEQKLISEEDLNSAVDHHHHHH
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:
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