Crystal structure of the human KLHL2 Kelch domain in complex with a WNK4 peptide. Determined by X-ray diffraction at 1.56 Å resolution. Released 8 Jan 2014.
Explore 4CHB in 3D Show helices and sheets RCSB PDB PDBe
4CHB contains 14 α-helices and 88 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 |
|---|---|---|---|
| β-strand | 307-312 | 6 | 1 |
| β-strand | 315 | 1 | 2 |
| β-strand | 319 | 1 | 2 |
| β-strand | 320 | 1 | 3 |
| β-strand | 323-327 | 5 | 1 |
| β-strand | 332-335 | 4 | 1 |
| α-helix | 338-339 | 2 | |
| β-strand | 343 | 1 | 3 |
| β-strand | 344 | 1 | 4 |
| β-strand | 347-351 | 5 | 5 |
| β-strand | 354-358 | 5 | 5 |
| β-strand | 361 | 1 | 4 |
| β-strand | 366 | 1 | 4 |
| β-strand | 370-374 | 5 | 5 |
| β-strand | 379-383 | 5 | 5 |
| α-helix | 384-386 | 3 | |
| β-strand | 391 | 1 | 6 |
| β-strand | 394-398 | 5 | 7 |
| β-strand | 401-405 | 5 | 7 |
| β-strand | 408 | 1 | 6 |
| β-strand | 413 | 1 | 6 |
| β-strand | 417-421 | 5 | 7 |
| β-strand | 426-430 | 5 | 7 |
| α-helix | 431-433 | 3 | |
| β-strand | 438 | 1 | 8 |
| β-strand | 441-445 | 5 | 9 |
| β-strand | 448-452 | 5 | 9 |
| β-strand | 455-456 | 2 | 8 |
| β-strand | 461-462 | 2 | 8 |
| β-strand | 466-470 | 5 | 9 |
| β-strand | 475-478 | 4 | 9 |
| α-helix | 480-482 | 3 | |
| β-strand | 487 | 1 | 10 |
| β-strand | 490-494 | 5 | 11 |
| β-strand | 497-501 | 5 | 11 |
| β-strand | 504-505 | 2 | 10 |
| β-strand | 508-509 | 2 | 10 |
| β-strand | 513-517 | 5 | 11 |
| β-strand | 522-525 | 4 | 11 |
| α-helix | 527-529 | 3 | |
| β-strand | 534 | 1 | 12 |
| β-strand | 537-541 | 5 | 13 |
| β-strand | 544-548 | 5 | 13 |
| β-strand | 551 | 1 | 12 |
| β-strand | 556 | 1 | 12 |
| β-strand | 560-564 | 5 | 13 |
| β-strand | 569-572 | 4 | 13 |
| α-helix | 576-577 | 2 | |
| β-strand | 582 | 1 | 2 |
| β-strand | 585-590 | 6 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 307-312 | 6 | 14 |
| β-strand | 315 | 1 | 15 |
| β-strand | 319 | 1 | 15 |
| β-strand | 320 | 1 | 16 |
| β-strand | 323-327 | 5 | 14 |
| β-strand | 332-336 | 5 | 14 |
| α-helix | 338-339 | 2 | |
| β-strand | 343 | 1 | 16 |
| β-strand | 344 | 1 | 17 |
| β-strand | 347-351 | 5 | 18 |
| β-strand | 354-358 | 5 | 18 |
| β-strand | 361 | 1 | 17 |
| β-strand | 366 | 1 | 17 |
| β-strand | 370-374 | 5 | 18 |
| β-strand | 379-383 | 5 | 18 |
| α-helix | 384-386 | 3 | |
| β-strand | 391 | 1 | 19 |
| β-strand | 394-398 | 5 | 20 |
| β-strand | 401-405 | 5 | 20 |
| β-strand | 408 | 1 | 19 |
| β-strand | 413 | 1 | 19 |
| β-strand | 417-421 | 5 | 20 |
| β-strand | 426-430 | 5 | 20 |
| α-helix | 431-433 | 3 | |
| β-strand | 438 | 1 | 21 |
| β-strand | 441-445 | 5 | 22 |
| β-strand | 448-452 | 5 | 22 |
| β-strand | 455-456 | 2 | 21 |
| β-strand | 461-462 | 2 | 21 |
| β-strand | 466-470 | 5 | 22 |
| β-strand | 475-478 | 4 | 22 |
| α-helix | 480-482 | 3 | |
| β-strand | 487 | 1 | 23 |
| β-strand | 490-494 | 5 | 24 |
| β-strand | 497-501 | 5 | 24 |
| β-strand | 504-505 | 2 | 23 |
| β-strand | 508-509 | 2 | 23 |
| β-strand | 513-517 | 5 | 24 |
| β-strand | 522-525 | 4 | 24 |
| α-helix | 527-529 | 3 | |
| β-strand | 534 | 1 | 25 |
| β-strand | 537-541 | 5 | 26 |
| β-strand | 544-548 | 5 | 26 |
| β-strand | 551 | 1 | 25 |
| β-strand | 556 | 1 | 25 |
| β-strand | 560-564 | 5 | 26 |
| β-strand | 569-572 | 4 | 26 |
| α-helix | 576-577 | 2 | |
| β-strand | 582 | 1 | 15 |
| β-strand | 585-590 | 6 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 562-564 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Kelch-like protein 2 | A, B | protein | 302 | HOMO SAPIENS | O95198 (AlphaFold model) |
| Serine/threonine-protein kinase WNK4 | C, D | protein | 11 | HOMO SAPIENS | Q96J92 (AlphaFold model) |
>4CHB_1 KELCH-LIKE PROTEIN 2 (chains A, B) SMSVRTRLRTPMNLPKLMVVVGGQAPKAIRSVECYDFKEERWHQVAELPSRRCRAGMVYM AGLVFAVGGFNGSLRVRTVDSYDPVKDQWTSVANMRDRRSTLGAAVLNGLLYAVGGFDGS TGLSSVEAYNIKSNEWFHVAPMNTRRSSVGVGVVGGLLYAVGGYDVASRQCLSTVECYNA TTNEWTYIAEMSTRRSGAGVGVLNNLLYAVGGHDGPLVRKSVEVYDPTTNAWRQVADMNM CRRNAGVCAVNGLLYVVGGDDGSCNLASVEYYNPTTDKWTVVSSCMSTGRSYAGVTVIDK RL
>4CHB_2 SERINE/THREONINE-PROTEIN KINASE WNK4 (chains C, D) EPEEPEADQHQ
Structural and Biochemical Characterisation of the Klhl3-Wnk Kinase Interaction Important in Blood Pressure Regulation. Schumacher, F., Sorrell, F.J., Alessi, D.R. et al. Biochem J (2014) 460:237. DOI 10.1042/BJ20140153 · PubMed
Other PDB entries of the same protein (UniProt O95198 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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