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AlphaFold monomer V2.0 prediction for mitochondrial import inner membrane translocase subunit TIM10 (P62072)

Analyse AlphaFold monomer V2.0 prediction for mitochondrial import inner membrane… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: P62072
Type: protein
Length: 90 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x7012c0b45c68a2c067644b9d3e5DDa06892c6957
Molecule: Mitochondrial import inner membrane translocase subunit TIM10
UniProt: P62072

Structure

1 distinct chain · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Mitochondrial import inner membrane translocase subunit TIM10	protein	90	81% helix, 0% strand	P62072

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

2BSK · Crystal structure of the TIM9 TIM10 hexameric complex · an experimental structure of the same protein · chain A against D, TM-score 0.79
2BSK · Crystal structure of the TIM9 Tim10 hexameric complex · an experimental structure of the same protein · chain A against D, TM-score 0.79
7CGP · Cryo-EM structure of the human mitochondrial translocase TIM22 complex at 3.7 angstrom. · an experimental structure of the same protein · chain A against O, TM-score 0.79
7CGP · Cryo-EM structure of the human mitochondrial translocase TIM22 complex at 3.7 ångström. · an experimental structure of the same protein · chain A against O, TM-score 0.79

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P62072
Elsewhere: UniProt P62072 · AlphaFold DB P62072

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