Human DRP-1 kinase, W305S S308A D40 mutant, crystal form with 3 monomers in the asymmetric unit. Determined by X-ray diffraction at 3.93 Å resolution. Released 24 Oct 2006.
Explore 1Z9X in 3D Show helices and sheets RCSB PDB PDBe
1Z9X contains 57 α-helices and 48 β-strands across 3 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 | 3-4 | 2 | |
| β-strand | 5 | 1 | 1 |
| α-helix | 9-12 | 4 | |
| β-strand | 13-21 | 9 | 1 |
| β-strand | 25-32 | 8 | 1 |
| β-strand | 37-45 | 9 | 1 |
| β-strand | 46 | 1 | 2 |
| α-helix | 47 | 1 | |
| β-strand | 56 | 1 | 2 |
| α-helix | 58-68 | 11 | |
| β-strand | 76 | 1 | 3 |
| β-strand | 79-84 | 6 | 1 |
| β-strand | 88-94 | 7 | 1 |
| β-strand | 100 | 1 | 3 |
| α-helix | 101-105 | 5 | |
| β-strand | 112 | 1 | 4 |
| α-helix | 113-132 | 20 | |
| β-strand | 135-136 | 2 | 5 |
| α-helix | 142-144 | 3 | |
| β-strand | 145-147 | 3 | 3 |
| α-helix | 155-156 | 2 | |
| β-strand | 157-159 | 3 | 3 |
| β-strand | 166-167 | 2 | 5 |
| α-helix | 168-169 | 2 | |
| α-helix | 181-183 | 3 | |
| α-helix | 186-189 | 4 | |
| α-helix | 197-212 | 16 | |
| α-helix | 222-230 | 9 | |
| α-helix | 238-241 | 4 | |
| α-helix | 246-253 | 8 | |
| α-helix | 264-265 | 2 | |
| α-helix | 266-271 | 6 | |
| α-helix | 280-288 | 9 | |
| β-strand | 290 | 1 | 4 |
| α-helix | 293-301 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-4 | 2 | |
| β-strand | 5 | 1 | 6 |
| α-helix | 9-12 | 4 | |
| β-strand | 13-21 | 9 | 6 |
| β-strand | 25-32 | 8 | 6 |
| β-strand | 37-45 | 9 | 6 |
| β-strand | 46 | 1 | 7 |
| α-helix | 47 | 1 | |
| β-strand | 56 | 1 | 7 |
| α-helix | 58-68 | 11 | |
| β-strand | 76 | 1 | 8 |
| β-strand | 79-84 | 6 | 6 |
| β-strand | 88-94 | 7 | 6 |
| β-strand | 100 | 1 | 8 |
| α-helix | 101-106 | 6 | |
| β-strand | 112 | 1 | 9 |
| α-helix | 113-132 | 20 | |
| β-strand | 135-136 | 2 | 10 |
| α-helix | 142-144 | 3 | |
| β-strand | 145-147 | 3 | 8 |
| α-helix | 155-156 | 2 | |
| β-strand | 157-159 | 3 | 8 |
| β-strand | 166-167 | 2 | 10 |
| α-helix | 168-169 | 2 | |
| α-helix | 181-183 | 3 | |
| α-helix | 186-189 | 4 | |
| α-helix | 197-212 | 16 | |
| α-helix | 222-230 | 9 | |
| α-helix | 238-241 | 4 | |
| α-helix | 246-253 | 8 | |
| α-helix | 264-265 | 2 | |
| α-helix | 266-271 | 6 | |
| α-helix | 280-288 | 9 | |
| β-strand | 290 | 1 | 9 |
| α-helix | 293-301 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-4 | 2 | |
| β-strand | 5 | 1 | 11 |
| α-helix | 9-12 | 4 | |
| β-strand | 13-21 | 9 | 11 |
| β-strand | 25-32 | 8 | 11 |
| β-strand | 37-45 | 9 | 11 |
| β-strand | 46 | 1 | 12 |
| α-helix | 47 | 1 | |
| β-strand | 56 | 1 | 12 |
| α-helix | 58-68 | 11 | |
| β-strand | 76 | 1 | 13 |
| β-strand | 79-84 | 6 | 11 |
| β-strand | 88-93 | 6 | 11 |
| β-strand | 100 | 1 | 13 |
| α-helix | 101-106 | 6 | |
| β-strand | 112 | 1 | 14 |
| α-helix | 113-132 | 20 | |
| β-strand | 135-136 | 2 | 15 |
| α-helix | 142-144 | 3 | |
| β-strand | 145-147 | 3 | 13 |
| α-helix | 155-156 | 2 | |
| β-strand | 157-159 | 3 | 13 |
| β-strand | 166-167 | 2 | 15 |
| α-helix | 168-169 | 2 | |
| α-helix | 181-183 | 3 | |
| α-helix | 186-189 | 4 | |
| α-helix | 197-212 | 16 | |
| α-helix | 222-230 | 9 | |
| α-helix | 238-241 | 4 | |
| α-helix | 246-253 | 8 | |
| α-helix | 264-265 | 2 | |
| α-helix | 266-271 | 6 | |
| α-helix | 280-288 | 9 | |
| β-strand | 290 | 1 | 14 |
| α-helix | 293-301 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Death-associated protein kinase 2 | A, B, C | protein | 321 | Homo sapiens | Q9UIK4 (AlphaFold model) |
>1Z9X_1 Death-associated protein kinase 2 (chains A, B, C) GMEPFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVSRE EIEREVSILRQVLHHNVITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSF IKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFG TPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITSVSYDFDEE FFSHTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDNQQAMVRRESVVNLENFRKQ YVRRRSKLAFSIVSLCNHLTR
A structural insight into the double-locking mechanism of the human death-associated DRP-1 kinase. Kursula, P., Lehmann, F., Shani, G. et al. To be published.
Other PDB entries of the same protein (UniProt Q9UIK4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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