5CUF: SeMet human Sestrin2

X-ray crystal structure of SeMet human Sestrin2. Determined by X-ray diffraction at 3.5 Å resolution. Released 13 Jan 2016.

Method
X-ray diffraction
Resolution
3.5 Å
Organism
Homo sapiens
Chains
5
Atoms
15,032
Mol. weight
277.21 kDa
Released
13 Jan 2016

Explore 5CUF in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5CUF contains 140 α-helices and 10 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: 28 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix68-725
α-helix78-836
α-helix87-10216
α-helix109-12113
α-helix126-13813
α-helix143-1475
α-helix149-1513
α-helix154-1574
α-helix159-16810
α-helix170-1723
α-helix175-1817
α-helix188-1903
α-helix191-21424
α-helix232-2354
α-helix257-27014
α-helix281-2833
α-helix284-2929
α-helix310-3156
α-helix334-3363
β-strand337-33821
α-helix339-3424
α-helix344-3485
α-helix349-3557
α-helix357-37216
α-helix387-40014
β-strand403-40421
α-helix412-4165
α-helix419-43012
α-helix437-4415
α-helix450-47627
Chain B: 28 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix68-725
α-helix78-836
α-helix87-10216
α-helix109-12113
α-helix126-13813
α-helix143-1475
α-helix149-1513
α-helix154-1574
α-helix159-16810
α-helix170-1723
α-helix175-1806
α-helix188-1903
α-helix191-21424
α-helix232-2354
α-helix257-26812
α-helix281-2833
α-helix284-2929
α-helix310-3156
α-helix334-3363
β-strand337-33822
α-helix339-3413
α-helix344-3485
α-helix349-3557
α-helix357-37216
α-helix387-40014
β-strand403-40422
α-helix412-4165
α-helix419-43012
α-helix437-4415
α-helix449-47628
Chains C, D and E: 28 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix68-725
α-helix78-836
α-helix87-10216
α-helix109-12113
α-helix126-13813
α-helix143-1475
α-helix149-1513
α-helix154-1574
α-helix159-16810
α-helix170-1723
α-helix175-1817
α-helix188-1903
α-helix191-21424
α-helix232-2354
α-helix257-26812
α-helix281-2833
α-helix284-2929
α-helix310-3156
α-helix334-3363
β-strand337-33823
α-helix339-3413
α-helix344-3485
α-helix349-3557
α-helix357-37216
α-helix387-40014
β-strand403-40423
α-helix412-4165
α-helix419-43012
α-helix437-4415
α-helix449-47628

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Sestrin-2A, B, C, D, Eprotein483Homo sapiensP58004 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E), FASTA
>5CUF_1 Sestrin-2 (chains A, B, C, D, E)
SNAMIVADSECRAELKDYLRFAPGGVGDSGPGEEQRESRARRGPRGPSAFIPVEEVLREG
AESLEQHLGLEALMSSGRVDNLAVVMGLHPDYFTSFWRLHYLLLHTDGPLASSWRHYIAI
MAAARHQCSYLVGSHMAEFLQTGGDPEWLLGLHRAPEKLRKLSEINKLLAHRPWLITKEH
IQALLKTGEHTWSLAELIQALVLLTHCHSLSSFVFGCGILPEGDADGSPAPQAPTPPSEQ
SSPPSRDPLNNSGGFESARDVEALMERMQQLQESLLRDEGTSQEEMESRFELEKSESLLV
TPSADILEPSPHPDMLCFVEDPTFGYEDFTRRGAQAPPTFRAQDYTWEDHGYSLIQRLYP
EGGQLLDEKFQAAYSLTYNTIAMHSGVDTSVLRRAIWNYIHCVFGIRYDDYDYGEVNQLL
ERNLKVYIKTVACYPEKTTRRMYNLFWRHFRHSEKVHVNLLLLEARMQAALLYALRAITR
YMT

Primary citation

Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domains. Kim, H., An, S., Ro, S.H. et al. Nat Commun (2015) 6:10025-10025. DOI 10.1038/ncomms10025 · PubMed

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

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