Calcium pump crystal structure with bound AlF4 and TG in the absence of calcium. Determined by X-ray diffraction at 2.55 Å resolution. Released 11 Dec 2007.
Explore 2ZBG in 3D Show helices and sheets RCSB PDB PDBe
2ZBG contains 55 α-helices and 33 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 | 4-6 | 3 | |
| α-helix | 9-16 | 8 | |
| α-helix | 26-36 | 11 | |
| α-helix | 41-43 | 3 | |
| α-helix | 45-48 | 4 | |
| α-helix | 49-57 | 9 | |
| α-helix | 60-74 | 15 | |
| α-helix | 90-109 | 20 | |
| α-helix | 115-119 | 5 | |
| α-helix | 120-122 | 3 | |
| β-strand | 126-129 | 4 | 1 |
| α-helix | 137 | 1 | |
| β-strand | 138-141 | 4 | 1 |
| α-helix | 142-144 | 3 | |
| β-strand | 150-154 | 5 | 1 |
| β-strand | 158 | 1 | 2 |
| β-strand | 162-168 | 7 | 1 |
| β-strand | 174-176 | 3 | 2 |
| α-helix | 178-181 | 4 | |
| β-strand | 186-188 | 3 | 2 |
| α-helix | 201-203 | 3 | |
| β-strand | 207-208 | 2 | 1 |
| β-strand | 213-216 | 4 | 2 |
| β-strand | 218-225 | 8 | 1 |
| α-helix | 227-229 | 3 | |
| α-helix | 231-240 | 10 | |
| α-helix | 244-247 | 4 | |
| α-helix | 248-273 | 26 | |
| α-helix | 288-306 | 19 | |
| α-helix | 311-328 | 18 | |
| β-strand | 332-333 | 2 | 3 |
| α-helix | 337-343 | 7 | |
| β-strand | 347-350 | 4 | 3 |
| β-strand | 357 | 1 | 4 |
| β-strand | 362-373 | 12 | 5 |
| β-strand | 376-384 | 9 | 5 |
| β-strand | 395-397 | 3 | 5 |
| β-strand | 400-401 | 2 | 5 |
| α-helix | 404-406 | 3 | |
| α-helix | 408-419 | 12 | |
| β-strand | 424-428 | 5 | 6 |
| β-strand | 433-437 | 5 | 6 |
| α-helix | 440-452 | 13 | |
| α-helix | 464-467 | 4 | |
| α-helix | 470-478 | 9 | |
| β-strand | 479-485 | 7 | 5 |
| β-strand | 493-500 | 8 | 5 |
| β-strand | 511-516 | 6 | 5 |
| α-helix | 518-523 | 6 | |
| β-strand | 525-530 | 6 | 5 |
| β-strand | 533-536 | 4 | 5 |
| α-helix | 539-553 | 15 | |
| β-strand | 560-567 | 8 | 5 |
| α-helix | 570-572 | 3 | |
| α-helix | 581-583 | 3 | |
| α-helix | 584-587 | 4 | |
| β-strand | 591-600 | 10 | 5 |
| α-helix | 602 | 1 | |
| β-strand | 603 | 1 | 4 |
| α-helix | 604 | 1 | |
| α-helix | 607-616 | 10 | |
| β-strand | 620-624 | 5 | 3 |
| α-helix | 629-639 | 11 | |
| β-strand | 652-654 | 3 | 3 |
| α-helix | 655-660 | 6 | |
| α-helix | 663-672 | 10 | |
| β-strand | 675-677 | 3 | 3 |
| α-helix | 681-692 | 12 | |
| β-strand | 698-702 | 5 | 3 |
| α-helix | 705-707 | 3 | |
| α-helix | 708-713 | 6 | |
| β-strand | 716-720 | 5 | 3 |
| α-helix | 725-730 | 6 | |
| β-strand | 733-735 | 3 | 3 |
| α-helix | 740-780 | 41 | |
| α-helix | 789-794 | 6 | |
| α-helix | 795-799 | 5 | |
| α-helix | 801-807 | 7 | |
| α-helix | 810-812 | 3 | |
| α-helix | 815-818 | 4 | |
| α-helix | 820-823 | 4 | |
| α-helix | 832-854 | 23 | |
| α-helix | 867-871 | 5 | |
| α-helix | 897-914 | 18 | |
| α-helix | 931-946 | 16 | |
| α-helix | 954-957 | 4 | |
| α-helix | 964-974 | 11 | |
| α-helix | 977-991 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 | A | protein | 995 | Oryctolagus cuniculus | P04191 (AlphaFold model) |
>2ZBG_1 Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (chains A) XMEAAHSKSTEECLAYFGVSETTGLTPDQVKRHLEKYGHNELPAEEGKSLWELVIEQFED LLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILIANAIVGVWQERNAENAIEAL KEYEPEMGKVYRADRKSVQRIKARDIVPGDIVEVAVGDKVPADIRILSIKSTTLRVDQSI LTGESVSVIKHTEPVPDPRAVNQDKKNMLFSGTNIAAGKALGIVATTGVSTEIGKIRDQM AATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWIRGAIYYFKIA VALAVAAIPEGLPAVITTCLALGTRRMAKKNAIVRSLPSVETLGCTSVICSDKTGTLTTN QMSVCKMFIIDKVDGDFCSLNEFSITGSTYAPEGEVLKNDKPIRSGQFDGLVELATICAL CNDSSLDFNETKGVYEKVGEATETALTTLVEKMNVFNTEVRNLSKVERANACNSVIRQLM KKEFTLEFSRDRKSMSVYCSPAKSSRAAVGNKMFVKGAPEGVIDRCNYVRVGTTRVPMTG PVKEKILSVIKEWGTGRDTLRCLALATRDTPPKREEMVLDDSSRFMEYETDLTFVGVVGM LDPPRKEVMGSIQLCRDAGIRVIMITGDNKGTAIAICRRIGIFGENEEVADRAYTGREFD DLPLAEQREACRRACCFARVEPSHKSKIVEYLQSYDEITAMTGDGVNDAPALKKAEIGIA MGSGTAVAKTASEMVLADDNFSTIVAAVEEGRAIYNNMKQFIRYLISSNVGEVVCIFLTA ALGLPEALIPVQLLWVNLVTDGLPATALGFNPPDLDIMDRPPRSPKEPLISGWLFFRYMA IGGYVGAATVGAAAWWFMYAEDGPGVTYHQLTHFMQCTEDHPHFEGLDCEIFEAPEPMTM ALSVLVTIEMCNALNSLSENQSLMRMPPWVNIWLLGSICLSMSLHFLILYVDPLPMIFKL KALDLTQWLMVLKISLPVIGLDEILKFIARNYLEG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ALF | Tetrafluoroaluminate ion | Al F4 | 1 |
| TG1 | Octanoic acid [3S-[3ALPHA, 3ABETA, 4ALPHA, 6BETA, 6ABETA, 7BETA, 8ALPHA(Z),… | C34 H50 O12 | 1 |
| MG | Magnesium ion | Mg | 1 |
How processing of aspartylphosphate is coupled to lumenal gating of the ion pathway in the calcium pump. Toyoshima, C., Norimatsu, Y., Iwasawa, S. et al. Proc Natl Acad Sci U S A (2007) 104:19831-19836. DOI 10.1073/pnas.0709978104 · PubMed
Other PDB entries of the same protein (UniProt P04191 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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