Structure of a human NHE1-CHP1 complex under pH 6.5. Determined by electron microscopy at 3.4 Å resolution. Released 23 Jun 2021.
Explore 7DSV in 3D Show helices and sheets RCSB PDB PDBe
7DSV contains 74 α-helices and 8 β-strands across 4 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 | 101-116 | 16 | |
| α-helix | 131-149 | 19 | |
| α-helix | 151-154 | 4 | |
| α-helix | 160 | 1 | |
| α-helix | 161-165 | 5 | |
| α-helix | 166-175 | 10 | |
| α-helix | 179-184 | 6 | |
| α-helix | 186-190 | 5 | |
| α-helix | 191-196 | 6 | |
| α-helix | 197-213 | 17 | |
| α-helix | 225-234 | 10 | |
| β-strand | 237 | 1 | 1 |
| α-helix | 239-244 | 6 | |
| α-helix | 253-280 | 28 | |
| α-helix | 288-319 | 32 | |
| α-helix | 330-347 | 18 | |
| α-helix | 352-366 | 15 | |
| α-helix | 373-403 | 31 | |
| α-helix | 411-437 | 27 | |
| α-helix | 443-445 | 3 | |
| α-helix | 446-453 | 8 | |
| β-strand | 458 | 1 | 1 |
| α-helix | 462-467 | 6 | |
| α-helix | 477-493 | 17 | |
| α-helix | 500-503 | 4 | |
| α-helix | 518-538 | 21 | |
| α-helix | 544-557 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 17-20 | 4 | |
| α-helix | 25-39 | 15 | |
| β-strand | 47 | 1 | 4 |
| α-helix | 48-52 | 5 | |
| α-helix | 63-70 | 8 | |
| β-strand | 77 | 1 | 4 |
| α-helix | 80-88 | 9 | |
| α-helix | 92-93 | 2 | |
| α-helix | 95-99 | 5 | |
| α-helix | 111-122 | 12 | |
| α-helix | 132-142 | 11 | |
| α-helix | 149-163 | 15 | |
| α-helix | 173-181 | 9 | |
| α-helix | 185-188 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sodium/hydrogen exchanger 1 | A, B | protein | 472 | Homo sapiens | P19634 (AlphaFold model) |
| Calcineurin B homologous protein 1 | C, D | protein | 185 | Homo sapiens | Q99653 (AlphaFold model) |
>7DSV_1 Sodium/hydrogen exchanger 1 (chains A, B) KAFPVLGIDYTHVRTPFEISLWILLACLMKIGFHVIPTISSIVPESCLLIVVGLLVGGLI KGVGETPPFLQSDVFFLFLLPPIILDAGYFLPLRQFTENLGTILIFAVVGTLWNAFFLGG LMYAVCLVGGEQINNIGLLDNLLFGSIISAVDPVAVLAVFEEIHINELLHILVFGESLLN DAVTVVLYHLFEEFANYEHVGIVDIFLGFLSFFVVALGGVLVGVVYGVIAAFTSRFTSHI RVIEPLFVFLYSYMAYLSAELFHLSGIMALIASGVVMRPYVEANISHKSHTTIKYFLKMW SSVSETLIFIFLGVSTVAGSHHWNWTFVISTLLFCLIARVLGVLGLTWFINKFRIVKLTP KDQFIIAYGGLRGAIAFSLGYLLDKKHFPMCDLFLTAIITVIFFTVFVQGMTIRPLVDLL AVKKKQETKRSINEEIHTQFLDHLLTGIEDICGHYGHHHWKDKLNRFNKKYV
>7DSV_2 Calcineurin B homologous protein 1 (chains C, D) DEELEEIKKETGFSHSQITRLYSRFTSLDKGENGTLSREDFQRIPELAINPLGDRIINAF FPEGEDQVNFRGFMRTLAHFRPIEDNEKSKDVNGPEPLNSRSNKLHFAFRLYDLDKDEKI SRDELLQVLRMMVGVNISDEQLGSIADRTIQEADQDGDSAASFTEFVKVLEKVDVEQKMS IRFLH
| ID | Name | Formula | Copies |
|---|---|---|---|
| LBN | 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine | C42 H82 N O8 P | 16 |
Structure and mechanism of the human NHE1-CHP1 complex. Dong, Y., Gao, Y., Ilie, A. et al. Nat Commun (2021) 12:3474-3474. DOI 10.1038/s41467-021-23496-z · 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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