NMR structure of a two-transmembrane segment TM VI-VII of NHE1. Determined by solution NMR. Released 2 Jul 2014.
Explore 2MDF in 3D Show helices and sheets RCSB PDB PDBe
2MDF contains 4 α-helices and 0 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 228 | 1 | |
| α-helix | 229-233 | 5 | |
| α-helix | 239-243 | 5 | |
| α-helix | 259-269 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium/hydrogen exchanger 1 | A | protein | 57 | Homo sapiens | P19634 (AlphaFold model) |
>2MDF_1 Sodium/hydrogen exchanger 1 (chains A) GSKKKDNLLFGSIISAVDPVAVLAVFEEIHINELLHILVFGESLLNDAVTVVLYKKK
Structural and Functional Analysis of the Transmembrane Segment Pair VI and VII of the NHE1 Isoform of the Na(+)/H(+) Exchanger. Alves, C., Lee, B.L., Sykes, B.D. et al. Biochemistry (2014) 53:3658-3670. DOI 10.1021/bi500392y · PubMed
Other PDB entries of the same protein (UniProt P19634 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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