3JC1: Increased Sodium Tolerance 1

Electron cryo-microscopy of the IST1-CHMP1B ESCRT-III copolymer. Determined by electron microscopy at 4.0 Å resolution. Released 16 Dec 2015.

Method
Electron microscopy
Resolution
4.0 Å
Organism
Homo sapiens
Chains
68
Atoms
92,106
Mol. weight
1321.66 kDa
Released
16 Dec 2015

Explore 3JC1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3JC1 contains 544 α-helices and 0 β-strands across 68 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.

Chains Aa, Ac, Ae, Ag, Ai, Ak, Am, Ao, Aq, As, Au, Aw, Ay, Ba, Bc, Be, Bg, Bi, Bk, Bm, Bo, Bq, Bs, Bu, Bw, By, Ca, Cc, Ce, Cg, Ci, Ck, Cm and Co: 11 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix8-4437
α-helix49-8133
α-helix83-864
α-helix99-1057
α-helix107-1104
α-helix116-12510
α-helix134-1407
α-helix146-1527
α-helix156-1583
α-helix159-17214
α-helix181-1855
Chains Ab, Ad, Af, Ah, Aj, Al, An, Ap, Ar, At, Av, Ax, Az, Bb, Bd, Bf, Bh, Bj, Bl, Bn, Bp, Br, Bt, Bv, Bx, Bz, Cb, Cd, Cf, Ch, Cj, Cl, Cn and Cp: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix2-3938
α-helix44-10158
α-helix105-13632
α-helix138-1403
α-helix143-15513

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Increased Sodium Tolerance 1 (IST1)Aa, Ac, Ae, Ag, Ai, Ak, Am, Ao, Aq, As, Au, Aw, Ay, Ba, Bc, Be, Bg, Bi, Bk, Bm, Bo, Bq, Bs, Bu, Bw, By, Ca, Cc, Ce, Cg, Ci, Ck, Cm, Coprotein182Homo sapiensP53990 (AlphaFold model)
Charged multivesicular body protein 1bAb, Ad, Af, Ah, Aj, Al, An, Ap, Ar, At, Av, Ax, Az, Bb, Bd, Bf, Bh, Bj, Bl, Bn, Bp, Br, Bt, Bv, Bx, Bz, Cb, Cd, Cf, Ch, Cj, Cl, Cn, Cpprotein160Homo sapiensQ7LBR1 (AlphaFold model)
Sequence of entity 1 (Aa, Ac, Ae, Ag, Ai, Ak, Am, Ao, Aq, As, Au, Aw, Ay, Ba, Bc, Be, Bg, Bi, Bk, Bm, Bo, Bq, Bs, Bu, Bw, By, Ca, Cc, Ce, Cg, Ci, Ck, Cm, Co), FASTA
>3JC1_1 Increased Sodium Tolerance 1 (IST1) (chains Aa, Ac, Ae, Ag, Ai, Ak, Am, Ao, Aq, As, Au, Aw, Ay, Ba, Bc, Be, Bg, Bi, Bk, Bm, Bo, Bq, Bs, Bu, Bw, By, Ca, Cc, Ce, Cg, Ci, Ck, Cm, Co)
FKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYL
VEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLC
AKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPDSVVMA
EA
Sequence of entity 2 (Ab, Ad, Af, Ah, Aj, Al, An, Ap, Ar, At, Av, Ax, Az, Bb, Bd, Bf, Bh, Bj, Bl, Bn, Bp, Br, Bt, Bv, Bx, Bz, Cb, Cd, Cf, Ch, Cj, Cl, Cn, Cp), FASTA
>3JC1_2 Charged multivesicular body protein 1b (chains Ab, Ad, Af, Ah, Aj, Al, An, Ap, Ar, At, Av, Ax, Az, Bb, Bd, Bf, Bh, Bj, Bl, Bn, Bp, Br, Bt, Bv, Bx, Bz, Cb, Cd, Cf, Ch, Cj, Cl, Cn, Cp)
MEKHLFNLKFAAKELSRSAKKCDKEEKAEKAKIEKAIQKGNMEVARIHAENAIRQKNQAV
NFLRMSARVDAVAARVQTAVTMGKVTKSMAGVVKSMDATLKTMNLEKISALMDKFEHQFE
TLDVQTQQMEDTMSSTTTLTTPQNQVDMLLQEMADEAGLD

Primary citation

Structure and membrane remodeling activity of ESCRT-III helical polymers. McCullough, J., Clippinger, A.K., Talledge, N. et al. Science (2015) 350:1548-1551. DOI 10.1126/science.aad8305 · PubMed

Other PDB entries of the same protein (UniProt P53990 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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