P53990: IST1 homolog (IST1)

IST1 homolog (IST1) is a 364-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: P53990.

Gene
IST1
Organism
Homo sapiens
Length
364 residues
Mean pLDDT
72.3
Model
AF-P53990-F1 v6
Model created
1 Aug 2025
PDB structures
16

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Model confidence (pLDDT)

The mean pLDDT of this model is 72.3 (confident overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate47%
70 to 90Confident: backbone generally right7%
50 to 70Low: treat with caution12%
Below 50Very low: often disordered regions33%

What pLDDT means and how to read it

Function

ESCRT-III-like protein involved in cytokinesis, nuclear envelope reassembly and endosomal tubulation (PubMed:19129479, PubMed:26040712, PubMed:28242692). Is required for efficient abscission during cytokinesis (PubMed:19129479). Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells (PubMed:19129479, PubMed:19129480). During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing (PubMed:26040712). Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (PubMed:28242692). Regulates…

Subunit structure

Interacts with CHMP1A, CHMP1B, VPS4A and VTA1. Interacts with SPAST, STAMBP, and USP8. May interact with VPS37B. May associate with the ESCRT-I complex. Interacts with MITD1, in competition with VSP4 (PubMed:23015756). Interacts with SPART (via MIT domain); leading to the recruitment of SPART to midbodies (PubMed:20719964). Interacts with SPAST (PubMed:23897888, PubMed:26040712)

Subcellular location

Cytoplasmic vesicle, Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, Midbody, Nucleus envelope

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
7S7JX-ray1.15 ÅB=342-364
4WZXX-ray1.39 ÅE=342-364
4U7EX-ray1.6 ÅA=341-364
4U7IX-ray1.79 ÅB=341-364
3FRRX-ray1.8 ÅA=1-189
4U7YX-ray2.5 ÅB=341-364
3FRSX-ray2.61 ÅA=5-189
8UC6X-ray2.7 ÅE/G=320-364
8V2SEM2.72 ÅB=1-364
6E8GEM2.9 ÅA/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/RB/S/TA/TB=1-364
8V2QEM2.95 ÅB=1-364
8V2REM3.01 ÅB=1-364
6TZ5EM3.1 ÅA/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=1-189
6TZ4EM3.2 Å01/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/SB=1-189
3JC1EM4.0 ÅAa/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=6-187
6TZAEM7.2 ÅA/B/C/D/E/F/G/H/I/J/K/L/M/N=1-189

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