Human leucine zipper- and sterile alpha motif-containing kinase (ZAK, MLT, HCCS-4, MRK, AZK, MLTK) in complex with vemurafenib. Determined by X-ray diffraction at 2.14 Å resolution. Released 30 Mar 2016.
Explore 5HES in 3D Show helices and sheets RCSB PDB PDBe
5HES contains 39 α-helices and 20 β-strands across 2 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 | 10 | 1 | 1 |
| α-helix | 13-15 | 3 | |
| β-strand | 16-21 | 6 | 1 |
| α-helix | 22-25 | 4 | |
| β-strand | 30-35 | 6 | 1 |
| α-helix | 36-38 | 3 | |
| β-strand | 40-47 | 8 | 1 |
| α-helix | 53-57 | 5 | |
| β-strand | 65 | 1 | 2 |
| α-helix | 66-67 | 2 | |
| β-strand | 68-74 | 7 | 1 |
| β-strand | 77-83 | 7 | 1 |
| β-strand | 88-89 | 2 | 2 |
| α-helix | 90-94 | 5 | |
| α-helix | 97-101 | 5 | |
| α-helix | 104-119 | 16 | |
| α-helix | 120-124 | 5 | |
| α-helix | 136-138 | 3 | |
| β-strand | 139-141 | 3 | 2 |
| β-strand | 147-149 | 3 | 2 |
| α-helix | 170-172 | 3 | |
| α-helix | 175-178 | 4 | |
| α-helix | 186-201 | 16 | |
| α-helix | 211-220 | 10 | |
| α-helix | 233-242 | 10 | |
| α-helix | 247-249 | 3 | |
| α-helix | 251-252 | 2 | |
| α-helix | 253-265 | 13 | |
| α-helix | 269-278 | 10 | |
| α-helix | 280-298 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-11 | 2 | 3 |
| α-helix | 13-15 | 3 | |
| β-strand | 16-21 | 6 | 3 |
| α-helix | 22-25 | 4 | |
| β-strand | 30-35 | 6 | 3 |
| β-strand | 40-47 | 8 | 3 |
| α-helix | 53-59 | 7 | |
| β-strand | 65 | 1 | 4 |
| α-helix | 66-67 | 2 | |
| β-strand | 68-74 | 7 | 3 |
| β-strand | 77-83 | 7 | 3 |
| β-strand | 89 | 1 | 4 |
| α-helix | 90-94 | 5 | |
| α-helix | 97-101 | 5 | |
| α-helix | 104-119 | 16 | |
| α-helix | 120-124 | 5 | |
| α-helix | 136-138 | 3 | |
| β-strand | 139-141 | 3 | 4 |
| β-strand | 147-149 | 3 | 4 |
| α-helix | 170-172 | 3 | |
| α-helix | 175-178 | 4 | |
| α-helix | 186-201 | 16 | |
| α-helix | 211-221 | 11 | |
| α-helix | 233-243 | 11 | |
| α-helix | 247-249 | 3 | |
| α-helix | 251-252 | 2 | |
| α-helix | 253-263 | 11 | |
| α-helix | 269-277 | 9 | |
| α-helix | 280-296 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mitogen-activated protein kinase kinase kinase MLT | A, B | protein | 307 | Homo sapiens | Q9NYL2 (AlphaFold model) |
>5HES_1 Mitogen-activated protein kinase kinase kinase MLT (chains A, B) SMGASFVQIKFDDLQFFENCGGGSFGSVYRAKWISQDKEVAVKKLLKIEKEAEILSVLSH RNIIQFYGVILEPPNYGIVTEYASLGSLYDYINSNRSEEMDMDHIMTWATDVAKGMHYLH MEAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFHNHTTHMSLVGTFPWMAPEVIQSLP VSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERLTIPSSCPRSFAELLHQC WEADAKKRPSFKQIISILESMSNDTSLPDKCNSFLHNKAEWRCEIEATLERLKKLERDLS FKEQELK
| ID | Name | Formula | Copies |
|---|---|---|---|
| 032 | N-(3-{[5-(4-chlorophenyl)-1H-pyrrolo[2,3-b]pyridin-3-yl]carbonyl}-2,4-difluorop… | C23 H18 Cl F2 N3 O3 S | 2 |
Water and common crystallization additives (EDO) are not listed.
Structure of the Human Protein Kinase ZAK in Complex with Vemurafenib. Mathea, S., Abdul Azeez, K.R., Salah, E. et al. ACS Chem Biol (2016) 11:1595-1602. DOI 10.1021/acschembio.6b00043 · PubMed
Other PDB entries of the same protein (UniProt Q9NYL2 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 5HES directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.