6TZ5: Charged multivesicular body protein 1b

CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1 (left-handed). Determined by electron microscopy at 3.1 Å resolution. Released 8 Apr 2020.

Method: Electron microscopy
Resolution: 3.1 Å
Organism: Homo sapiens
Chains: 68
Atoms: 93,500
Mol. weight: 1486.3 kDa
Released: 8 Apr 2020

Explore 6TZ5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6TZ5 contains 510 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 A, BA, BB, C, DA, DB, E, FA, FB, G, HA, HB, I, JA, JB, K, LA, LB, M, NA, NB, O, PA, PB, Q, RA, S, TA, V, VA, X, XA, Z and ZA: 10 helices, 0 β-strands

Element	Residues	Length
α-helix	8-45	38
α-helix	50-81	32
α-helix	83-88	6
α-helix	94-96	3
α-helix	97-105	9
α-helix	116-126	11
α-helix	134-139	6
α-helix	146-151	6
α-helix	159-173	15
α-helix	181-185	5

Chains AA, AB, B, CA, CB, D, EA, EB, F, GA, GB, H, IA, IB, J, KA, KB, L, MA, MB, N, OA, OB, P, QA, QB, R, SA, T, UA, W, WA, Y and YA: 5 helices, 0 β-strands

Element	Residues	Length
α-helix	4-42	39
α-helix	45-105	61
α-helix	108-139	32
α-helix	146-160	15
α-helix	188-197	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Charged multivesicular body protein 1b	AA, AB, B, CA, CB, D, EA, EB, F, GA, GB, H, IA, IB, J, KA, KB, L, MA, MB, N, OA, OB, P, QA, QB, R, SA, T, UA, W, WA, Y, YA	protein	199	Homo sapiens	Q7LBR1 (AlphaFold model)
IST1 homolog	A, BA, BB, C, DA, DB, E, FA, FB, G, HA, HB, I, JA, JB, K, LA, LB, M, NA, NB, O, PA, PB, Q, RA, S, TA, V, VA, X, XA, Z, ZA	protein	189	Homo sapiens	P53990 (AlphaFold model)

Sequence of entity 1 (AA, AB, B, CA, CB, D, EA, EB, F, GA, GB, H, IA, IB, J, KA, KB, L, MA, MB, N, OA, OB, P, QA, QB, R, SA, T, UA, W, WA, Y, YA), FASTA

>6TZ5_1 Charged multivesicular body protein 1b (chains AA, AB, B, CA, CB, D, EA, EB, F, GA, GB, H, IA, IB, J, KA, KB, L, MA, MB, N, OA, OB, P, QA, QB, R, SA, T, UA, W, WA, Y, YA)
MSNMEKHLFNLKFAAKELSRSAKKCDKEEKAEKAKIEKAIQKGNMEVARIHAENAIRQKN
QAVNFLRMSARVDAVAARVQTAVTMGKVTKSMAGVVKSMDATLKTMNLEKISALMDKFEH
QFETLDVQTQQMEDTMSSTTTLTTPQNQVDMLLQEMADEAGLDLNMELPQGQTGSVGTSV
ASAEQDELSQRLARLRDQV

Sequence of entity 2 (A, BA, BB, C, DA, DB, E, FA, FB, G, HA, HB, I, JA, JB, K, LA, LB, M, NA, NB, O, PA, PB, Q, RA, S, TA, V, VA, X, XA, Z, ZA), FASTA

>6TZ5_2 IST1 homolog (chains A, BA, BB, C, DA, DB, E, FA, FB, G, HA, HB, I, JA, JB, K, LA, LB, M, NA, NB, O, PA, PB, Q, RA, S, TA, V, VA, X, XA, Z, ZA)
MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHII
REDYLVEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIV
ADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPD
SVVMAEAPP

Primary citation

Membrane constriction and thinning by sequential ESCRT-III polymerization. Nguyen, H.C., Talledge, N., McCullough, J. et al. Nat Struct Mol Biol (2020) 27:392-399. DOI 10.1038/s41594-020-0404-x · PubMed

Other PDB entries of the same protein (UniProt Q7LBR1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4TXR 1.0 Å, Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM and CHMP5 MIM
4TXQ 2.21 Å, Crystal structure of LIP5 N-terminal domain complexed with CHMP1B MIM
3EAB 2.5 Å, Crystal structure of Spastin MIT in complex with ESCRT III
8V2S 2.72 Å, CHMP1B/IST1 dsDNA bound copolymer
6E8G 2.9 Å, CryoEM reconstruction of IST1-CHMP1B copolymer filament bound to ssDNA at 2.9 Angstrom…
8V2Q 2.95 Å, CHMP1B/IST1 ssRNA bound copolymer
8V2R 3.01 Å, CHMP1B/IST1 ssDNA bound copolymer
6TZ4 3.2 Å, CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B+IST1…
3JC1 4.0 Å, Electron cryo-microscopy of the IST1-CHMP1B ESCRT-III copolymer
6TZ9 6.2 Å, CryoEM reconstruction of membrane-bound ESCRT-III filament composed of CHMP1B only

Browse structure collections

About this viewer

MolViewer shows 6TZ5 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.