5DJ4: Leucine-bound Sestrin2 from Homo sapiens
Leucine-bound Sestrin2 from Homo sapiens. Determined by X-ray diffraction at 2.7 Å resolution. Released 25 Nov 2015.
- Method
- X-ray diffraction
- Resolution
- 2.7 Å
- Organism
- Homo sapiens
- Chains
- 5
- Atoms
- 14,911
- Mol. weight
- 273.46 kDa
- Ligands
- LEU
- Released
- 25 Nov 2015
Explore 5DJ4 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
5DJ4 contains 137 α-helices and 30 β-strands across 5 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.
Chain A: 27 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 68-71 | 4 | |
| α-helix | 78-83 | 6 | |
| α-helix | 87-102 | 16 | |
| α-helix | 109-121 | 13 | |
| α-helix | 126-138 | 13 | |
| α-helix | 143-147 | 5 | |
| α-helix | 149-151 | 3 | |
| α-helix | 154-157 | 4 | |
| α-helix | 160-168 | 9 | |
| α-helix | 170-172 | 3 | |
| α-helix | 175-182 | 8 | |
| α-helix | 191-213 | 23 | |
| β-strand | 216 | 1 | 1 |
| α-helix | 217-218 | 2 | |
| β-strand | 235 | 1 | 1 |
| α-helix | 257-270 | 14 | |
| α-helix | 283-292 | 10 | |
| α-helix | 313-315 | 3 | |
| α-helix | 334-336 | 3 | |
| β-strand | 337-338 | 2 | 2 |
| α-helix | 339-341 | 3 | |
| α-helix | 344-348 | 5 | |
| α-helix | 349-355 | 7 | |
| α-helix | 357-371 | 15 | |
| β-strand | 377 | 1 | 3 |
| β-strand | 382 | 1 | 3 |
| α-helix | 387-400 | 14 | |
| β-strand | 403-404 | 2 | 2 |
| α-helix | 411-416 | 6 | |
| α-helix | 419-430 | 12 | |
| α-helix | 432-434 | 3 | |
| α-helix | 437-442 | 6 | |
| α-helix | 449-479 | 31 | |
Chain B: 28 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 68-71 | 4 | |
| α-helix | 78-83 | 6 | |
| α-helix | 87-102 | 16 | |
| α-helix | 109-121 | 13 | |
| α-helix | 126-138 | 13 | |
| α-helix | 143-147 | 5 | |
| α-helix | 149-151 | 3 | |
| α-helix | 154-157 | 4 | |
| α-helix | 160-168 | 9 | |
| α-helix | 170-172 | 3 | |
| α-helix | 175-182 | 8 | |
| α-helix | 188-190 | 3 | |
| α-helix | 191-213 | 23 | |
| β-strand | 216 | 1 | 4 |
| α-helix | 217-219 | 3 | |
| β-strand | 235 | 1 | 4 |
| α-helix | 257-269 | 13 | |
| α-helix | 283-292 | 10 | |
| α-helix | 313-315 | 3 | |
| α-helix | 334-336 | 3 | |
| β-strand | 337-338 | 2 | 5 |
| α-helix | 339-341 | 3 | |
| α-helix | 344-348 | 5 | |
| α-helix | 349-355 | 7 | |
| α-helix | 357-371 | 15 | |
| β-strand | 377-378 | 2 | 6 |
| β-strand | 381-382 | 2 | 6 |
| α-helix | 387-400 | 14 | |
| β-strand | 403-404 | 2 | 5 |
| α-helix | 411-416 | 6 | |
| α-helix | 419-430 | 12 | |
| α-helix | 432-434 | 3 | |
| α-helix | 437-442 | 6 | |
| α-helix | 449-478 | 30 | |
Chain C: 27 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 68-71 | 4 | |
| α-helix | 78-83 | 6 | |
| α-helix | 87-102 | 16 | |
| α-helix | 109-121 | 13 | |
| α-helix | 126-138 | 13 | |
| α-helix | 143-147 | 5 | |
| α-helix | 149-151 | 3 | |
| α-helix | 154-157 | 4 | |
| α-helix | 160-168 | 9 | |
| α-helix | 170-172 | 3 | |
| α-helix | 175-182 | 8 | |
| α-helix | 191-214 | 24 | |
| β-strand | 216 | 1 | 7 |
| α-helix | 217-219 | 3 | |
| β-strand | 235 | 1 | 7 |
| α-helix | 257-268 | 12 | |
| α-helix | 283-292 | 10 | |
| α-helix | 313-315 | 3 | |
| α-helix | 334-336 | 3 | |
| β-strand | 337-338 | 2 | 8 |
| α-helix | 339-341 | 3 | |
| α-helix | 344-348 | 5 | |
| α-helix | 349-355 | 7 | |
| α-helix | 357-372 | 16 | |
| β-strand | 377-378 | 2 | 9 |
| β-strand | 381-382 | 2 | 9 |
| α-helix | 387-400 | 14 | |
| β-strand | 403-404 | 2 | 8 |
| α-helix | 411-416 | 6 | |
| α-helix | 419-430 | 12 | |
| α-helix | 432-434 | 3 | |
| α-helix | 437-442 | 6 | |
| α-helix | 449-479 | 31 | |
Chain D: 27 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 68-71 | 4 | |
| α-helix | 78-83 | 6 | |
| α-helix | 87-102 | 16 | |
| α-helix | 109-121 | 13 | |
| α-helix | 126-138 | 13 | |
| α-helix | 143-147 | 5 | |
| α-helix | 149-151 | 3 | |
| α-helix | 154-157 | 4 | |
| α-helix | 160-168 | 9 | |
| α-helix | 170-172 | 3 | |
| α-helix | 175-182 | 8 | |
| α-helix | 191-214 | 24 | |
| β-strand | 216 | 1 | 10 |
| α-helix | 217-218 | 2 | |
| β-strand | 235 | 1 | 10 |
| α-helix | 257-266 | 10 | |
| α-helix | 285-291 | 7 | |
| α-helix | 313-315 | 3 | |
| α-helix | 334-336 | 3 | |
| β-strand | 337-338 | 2 | 11 |
| α-helix | 339-341 | 3 | |
| α-helix | 344-348 | 5 | |
| α-helix | 349-355 | 7 | |
| α-helix | 357-372 | 16 | |
| β-strand | 377-378 | 2 | 12 |
| β-strand | 381-382 | 2 | 12 |
| α-helix | 387-400 | 14 | |
| β-strand | 403-404 | 2 | 11 |
| α-helix | 411-416 | 6 | |
| α-helix | 419-430 | 12 | |
| α-helix | 432-434 | 3 | |
| α-helix | 437-442 | 6 | |
| α-helix | 449-478 | 30 | |
Chain E: 28 helices, 6 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 68-71 | 4 | |
| α-helix | 78-83 | 6 | |
| α-helix | 87-102 | 16 | |
| α-helix | 109-120 | 12 | |
| α-helix | 121-123 | 3 | |
| α-helix | 126-138 | 13 | |
| α-helix | 143-147 | 5 | |
| α-helix | 149-151 | 3 | |
| α-helix | 154-157 | 4 | |
| α-helix | 160-168 | 9 | |
| α-helix | 170-172 | 3 | |
| α-helix | 175-181 | 7 | |
| α-helix | 188-190 | 3 | |
| α-helix | 191-213 | 23 | |
| β-strand | 216 | 1 | 13 |
| α-helix | 217-218 | 2 | |
| β-strand | 235 | 1 | 13 |
| α-helix | 257-267 | 11 | |
| α-helix | 283-292 | 10 | |
| α-helix | 313-315 | 3 | |
| α-helix | 334-336 | 3 | |
| β-strand | 337-338 | 2 | 14 |
| α-helix | 344-348 | 5 | |
| α-helix | 349-355 | 7 | |
| α-helix | 357-372 | 16 | |
| β-strand | 377-378 | 2 | 15 |
| β-strand | 381-382 | 2 | 15 |
| α-helix | 387-400 | 14 | |
| β-strand | 403-404 | 2 | 14 |
| α-helix | 412-416 | 5 | |
| α-helix | 419-430 | 12 | |
| α-helix | 432-434 | 3 | |
| α-helix | 437-442 | 6 | |
| α-helix | 449-479 | 31 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Sestrin-2 | A, B, C, D, E | protein | 480 | Homo sapiens | P58004 (AlphaFold model) |
Sequence of entity 1 (A, B, C, D, E), FASTA
>5DJ4_1 Sestrin-2 (chains A, B, C, D, E)
MIVADSECRAELKDYLRFAPGGVGDSGPGEEQRESRARRGPRGPSAFIPVEEVLREGAES
LEQHLGLEALMSSGRVDNLAVVMGLHPDYFTSFWRLHYLLLHTDGPLASSWRHYIAIMAA
ARHQCSYLVGSHMAEFLQTGGDPEWLLGLHRAPEKLRKLSEINKLLAHRPWLITKEHIQA
LLKTGEHTWSLAELIQALVLLTHCHSLSSFVFGCGILPEGDADGSPAPQAPTPPSEQSSP
PSRDPLNNSGGFESARDVEALMERMQQLQESLLRDEGTSQEEMESRFELEKSESLLVTPS
ADILEPSPHPDMLCFVEDPTFGYEDFTRRGAQAPPTFRAQDYTWEDHGYSLIQRLYPEGG
QLLDEKFQAAYSLTYNTIAMHSGVDTSVLRRAIWNYIHCVFGIRYDDYDYGEVNQLLERN
LKVYIKTVACYPEKTTRRMYNLFWRHFRHSEKVHVNLLLLEARMQAALLYALRAITRYMT
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| LEU | Leucine | C6 H13 N O2 | 5 |
Primary citation
Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway. Saxton, R.A., Knockenhauer, K.E., Wolfson, R.L. et al. Science (2016) 351:53-58. DOI 10.1126/science.aad2087 · PubMed
Other PDB entries of the same protein (UniProt P58004 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 9PDM 2.7 Å, Leucine-bound Sestrin2 from Homo sapiens (GATOR2-inspired update)
- 5T0N 3.0 Å, Pseudo-apo structure of Sestrin2 at 3.0 angstrom resolution
- 6N0M 3.3 Å, Crystal structure of SESTRIN2 in complex with nv-0005138
- 9DX1 3.36 Å, Human GATOR2 complex - Sestrin2 bound state
- 9LWF 3.41 Å, Cryo-EM structure of dual sensor bound GATOR2 complex
- 5CUF 3.5 Å, X-ray crystal structure of SeMet human Sestrin2
- 9LVJ 3.82 Å, Cryo-EM structure of Sestrin2 bound human GATOR2 complex
Browse structure collections
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