Cryo-EM structure of the human inward-rectifier potassium 2.1 channel (Kir2.1). Determined by electron microscopy at 4.3 Å resolution. Released 28 Sept 2022.
Explore 7ZDZ in 3D Show helices and sheets RCSB PDB PDBe
7ZDZ contains 30 α-helices and 68 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 | 56-58 | 3 | |
| α-helix | 73-78 | 6 | |
| α-helix | 84-109 | 26 | |
| α-helix | 129-140 | 12 | |
| α-helix | 155-184 | 30 | |
| β-strand | 193-194 | 2 | 1 |
| β-strand | 199-204 | 6 | 2 |
| β-strand | 207-211 | 5 | 2 |
| β-strand | 212-213 | 2 | 3 |
| β-strand | 215-216 | 2 | 1 |
| β-strand | 222-223 | 2 | 4 |
| β-strand | 228-236 | 9 | 5 |
| β-strand | 242-249 | 8 | 5 |
| β-strand | 268-269 | 2 | 3 |
| α-helix | 284-289 | 6 | |
| β-strand | 293-297 | 5 | 5 |
| β-strand | 300-302 | 3 | 4 |
| β-strand | 308-309 | 2 | 4 |
| β-strand | 312-313 | 2 | 5 |
| β-strand | 320-322 | 3 | 2 |
| β-strand | 325 | 1 | 6 |
| α-helix | 331 | 1 | |
| β-strand | 332 | 1 | 7 |
| α-helix | 333 | 1 | |
| β-strand | 337 | 1 | 7 |
| β-strand | 348 | 1 | 6 |
| α-helix | 358-365 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 57-58 | 2 | 8 |
| α-helix | 61-63 | 3 | |
| α-helix | 73-79 | 7 | |
| α-helix | 84-114 | 31 | |
| α-helix | 128-140 | 13 | |
| α-helix | 155-184 | 30 | |
| β-strand | 194 | 1 | 9 |
| β-strand | 202-204 | 3 | 10 |
| β-strand | 207-212 | 6 | 10 |
| β-strand | 215 | 1 | 9 |
| β-strand | 222-223 | 2 | 11 |
| β-strand | 228-236 | 9 | 12 |
| β-strand | 242-249 | 8 | 12 |
| β-strand | 269-272 | 4 | 10 |
| α-helix | 284-289 | 6 | |
| β-strand | 293-297 | 5 | 12 |
| β-strand | 300-302 | 3 | 11 |
| β-strand | 308-309 | 2 | 11 |
| β-strand | 312 | 1 | 12 |
| β-strand | 315-316 | 2 | 12 |
| β-strand | 324-325 | 2 | 13 |
| β-strand | 330-333 | 4 | 14 |
| β-strand | 336-339 | 4 | 14 |
| α-helix | 341-343 | 3 | |
| β-strand | 348-349 | 2 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 74-78 | 5 | |
| α-helix | 84-110 | 27 | |
| α-helix | 129-140 | 12 | |
| α-helix | 155-180 | 26 | |
| α-helix | 181-183 | 3 | |
| β-strand | 194-195 | 2 | 15 |
| β-strand | 200-204 | 5 | 16 |
| β-strand | 207-213 | 7 | 16 |
| β-strand | 214-215 | 2 | 15 |
| β-strand | 222-236 | 15 | 17 |
| β-strand | 242-249 | 8 | 17 |
| β-strand | 268-271 | 4 | 16 |
| α-helix | 284-288 | 5 | |
| β-strand | 293-302 | 10 | 17 |
| β-strand | 308-315 | 8 | 17 |
| β-strand | 325-326 | 2 | 18 |
| α-helix | 327-328 | 2 | |
| β-strand | 338-339 | 2 | 8 |
| α-helix | 341-343 | 3 | |
| β-strand | 347-348 | 2 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 71-109 | 39 | |
| α-helix | 112-114 | 3 | |
| α-helix | 130-140 | 11 | |
| α-helix | 155-183 | 29 | |
| β-strand | 193-195 | 3 | 19 |
| β-strand | 199 | 1 | 20 |
| β-strand | 200-204 | 5 | 21 |
| β-strand | 207-211 | 5 | 21 |
| β-strand | 212-213 | 2 | 22 |
| β-strand | 214-216 | 3 | 19 |
| β-strand | 223 | 1 | 23 |
| β-strand | 228-236 | 9 | 24 |
| β-strand | 242-249 | 8 | 24 |
| β-strand | 268-269 | 2 | 22 |
| β-strand | 272 | 1 | 21 |
| α-helix | 284-289 | 6 | |
| β-strand | 293-297 | 5 | 24 |
| β-strand | 300-301 | 2 | 23 |
| β-strand | 308-309 | 2 | 23 |
| β-strand | 312-315 | 4 | 24 |
| β-strand | 320 | 1 | 20 |
| β-strand | 324-325 | 2 | 25 |
| β-strand | 332 | 1 | 26 |
| β-strand | 337 | 1 | 26 |
| β-strand | 348-349 | 2 | 25 |
| α-helix | 358-363 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Inward rectifier potassium channel 2 | A, B, C, D | protein | 427 | Homo sapiens | P63252 (AlphaFold model) |
>7ZDZ_1 Inward rectifier potassium channel 2 (chains A, B, C, D) MGSVRTNRYSIVSSEEDGMKLATMAVANGFGNGKSKVHTRQQCRSRFVKKDGHCNVQFIN VGEKGQRYLADIFTTCVDIRWRWMLVIFCLAFVLSWLFFGCVFWLIALLHGDLDASKEGK ACVSEVNSFTAAFLFSIETQTTIGYGFRCVTDECPIAVFMVVFQSIVGCIIDAFIIGAVM AKMAKPKKRNETLVFSHNAVIAMRDGKLCLMWRVGNLRKSHLVEAHVRAQLLKSRITSEG EYIPLDQIDINVGFDSGIDRIFLVSPITIVHEIDEDSPLYDLSKQDIDNADFEIVVILEG MVEATAMTTQCRSSYLANEILWGHRYEPVLFEEKHYYKVDYSRFHKTYEVPNTPLCSARD LAEKKYILSNANSFCYENEVALTSKEEDDSENGVPESTSTDTPPDIDLHNQASVPLEPRP LRRESEI
| ID | Name | Formula | Copies |
|---|---|---|---|
| SR | Strontium ion | Sr | 2 |
Water and common crystallization additives (K) are not listed.
Cryo-electron microscopy unveils unique structural features of the human Kir2.1 channel. Fernandes, C.A.H., Zuniga, D., Fagnen, C. et al. Sci Adv (2022) 8:eabq8489-eabq8489. DOI 10.1126/sciadv.abq8489 · PubMed
Other PDB entries of the same protein (UniProt P63252 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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