Structure of the Tandem MA-3 Region of Pdcd4. Determined by solution NMR. Released 16 Mar 2011.
Explore 2KZT in 3D Show helices and sheets RCSB PDB PDBe
2KZT contains 20 α-helices and 2 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 |
|---|---|---|---|
| α-helix | 157-158 | 2 | |
| α-helix | 161-178 | 18 | |
| α-helix | 181-191 | 11 | |
| α-helix | 195-198 | 4 | |
| α-helix | 199-210 | 12 | |
| α-helix | 213-226 | 14 | |
| β-strand | 227 | 1 | 1 |
| β-strand | 231 | 1 | 1 |
| α-helix | 233-253 | 21 | |
| α-helix | 257-271 | 15 | |
| α-helix | 278-281 | 4 | |
| α-helix | 289-305 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 321-325 | 5 | |
| α-helix | 331-336 | 6 | |
| α-helix | 337-341 | 5 | |
| α-helix | 344-351 | 8 | |
| α-helix | 358-360 | 3 | |
| α-helix | 361-373 | 13 | |
| α-helix | 377-392 | 16 | |
| α-helix | 398-416 | 19 | |
| α-helix | 423-436 | 14 | |
| α-helix | 441-444 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Programmed cell death protein 4 | A | protein | 163 | Homo sapiens | Q53EL6 (AlphaFold model) |
| Programmed cell death protein 4 | B | protein | 131 | Mus musculus | Q61823 (AlphaFold model) |
>2KZT_1 Programmed cell death protein 4 (chains A) GLPLDERAFEKTLTPIIQEYFEHGDTNEVAEMLRDLNLGEMKSGVPVLAVSLALEGKASH REMTSKLLSDLCGTVMSTTDVEKSFDKLLKDLPELALDTPRAPQLVGQFIARAVGDGILC NTYIDSYKGTVDCVQARAALDKATVLLSMSKGGKRKDSVWGSG
>2KZT_2 Programmed cell death protein 4 (chains B) GGQQPVNHLVKEIDMLLKEYLLSGDISEAEHCLKELEVPHFHHELVYEAIVMVLESTGES AFKMILDLLKSLWKSSTITIDQMKRGYERIYNEIPDINLDVPHSYSVLERFVEECFQAGI ISKQLRDLCPS
Structure of the tandem MA-3 region of Pdcd4 protein and characterization of its interactions with eIF4A and eIF4G: molecular mechanisms of a tumor suppressor. Waters, L.C., Strong, S.L., Ferlemann, E. et al. J Biol Chem (2011) 286:17270-17280. DOI 10.1074/jbc.M110.166157 · PubMed
Other PDB entries of the same protein (UniProt Q53EL6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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