6N0M: SESTRIN2

Crystal structure of SESTRIN2 in complex with nv-0005138. Determined by X-ray diffraction at 3.3 Å resolution. Released 10 Apr 2019.

Method: X-ray diffraction
Resolution: 3.3 Å
Organism: Homo sapiens
Chains: 5
Atoms: 14,811
Mol. weight: 238.2 kDa
Ligands: K94
Released: 10 Apr 2019

Explore 6N0M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6N0M contains 127 α-helices and 28 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: 26 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	68-73	6
α-helix	78-84	7
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	159-168	10
α-helix	170-172	3
α-helix	175-182	8
α-helix	191-213	23
β-strand	216	1	1
β-strand	235	1	1
α-helix	257-270	14
α-helix	282-292	11
α-helix	312-315	4
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	378	1	3
β-strand	381	1	3
α-helix	387-400	14
β-strand	403-404	2	2
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

Chain B: 26 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	68-73	6
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	159-168	10
α-helix	170-172	3
α-helix	175-181	7
α-helix	188-190	3
α-helix	191-213	23
β-strand	216	1	4
β-strand	235	1	4
α-helix	258-269	12
α-helix	282-292	11
α-helix	312-315	4
β-strand	337-338	2	5
α-helix	339-341	3
α-helix	344-348	5
α-helix	349-355	7
α-helix	357-372	16
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	449-479	31

Chain C: 25 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	68-73	6
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	154-168	15
α-helix	170-172	3
α-helix	175-182	8
α-helix	191-214	24
β-strand	216	1	6
β-strand	235	1	6
α-helix	257-267	11
α-helix	284-292	9
α-helix	312-315	4
α-helix	334-336	3
β-strand	338	1	7
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	8
β-strand	381-382	2	8
α-helix	387-400	14
β-strand	404	1	7
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: 24 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	68-73	6
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	154-168	15
α-helix	170-172	3
α-helix	175-182	8
α-helix	188-190	3
α-helix	191-213	23
β-strand	216	1	9
β-strand	235	1	9
α-helix	257-267	11
α-helix	283-292	10
α-helix	312-315	4
β-strand	337-338	2	10
α-helix	344-348	5
α-helix	349-355	7
α-helix	357-372	16
β-strand	377-378	2	11
β-strand	381-382	2	11
α-helix	387-400	14
β-strand	403-404	2	10
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

Chain E: 26 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	68-73	6
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	154-168	15
α-helix	170-172	3
α-helix	175-181	7
α-helix	191-213	23
β-strand	216	1	12
α-helix	217-218	2
β-strand	235	1	12
α-helix	257-268	12
α-helix	282-292	11
α-helix	312-315	4
α-helix	334-336	3
β-strand	338	1	13
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	14
β-strand	381-382	2	14
α-helix	387-400	14
β-strand	404	1	13
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

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Sestrin-2	A, B, C, D, E	protein	415	Homo sapiens	P58004 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E), FASTA

>6N0M_1 Sestrin-2 (chains A, B, C, D, E)
GLEALMSSGRVDNLAVVMGLHPDYFTSFWRLHYLLLHTDGPLASSWRHYIAIMAAARHQC
SYLVGSHMAEFLQTGGDPEWLLGLHRAPEKLRKLSEINKLLAHRPWLITKEHIQALLKTG
EHTWSLAELIQALVLLTHCHSLSSFVFGCGILPEGDADGSPAPQAPTPPSEQSSPPSRDP
LNNSGGFESARDVEALMERMQQLQESLLRDEGTSQEEMESRFELEKSESLLVTPSADILE
PSPHPDMLCFVEDPTFGYEDFTRRGAQAPPTFRAQDYTWEDHGYSLIQRLYPEGGQLLDE
KFQAAYSLTYNTIAMHSGVDTSVLRRAIWNYIHCVFGIRYDDYDYGEVNQLLERNLKVYI
KTVACYPEKTTRRMYNLFWRHFRHSEKVHVNLLLLEARMQAALLYALRAITRYMT

Ligands and cofactors

ID	Name	Formula	Copies
K94	4-(difluoromethyl)-L-leucine	C7 H13 F2 N O2	5

Primary citation

Discovery of NV-5138, the first selective Brain mTORC1 activator. Sengupta, S., Giaime, E., Narayan, S. et al. Sci Rep (2019) 9:4107-4107. DOI 10.1038/s41598-019-40693-5 · PubMed

Other PDB entries of the same protein (UniProt P58004 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5DJ4 2.7 Å, Leucine-bound Sestrin2 from Homo sapiens
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
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

About this viewer

MolViewer shows 6N0M 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.