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Structure of the ims domain of the mitochondrial import protein TIM21 from S. cerevisiae
Analyse Structure of the ims domain of the mitochondrial import protein TIM21 from S.… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2CIU
- Type
- protein
- Length
- 123 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Import inner membrane translocase subunit TIM21 mitochondrial
- UniProt
- P53220
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Import inner membrane translocase subunit TIM21 mitochondrial | protein | 123 | 17% helix, 39% strand | P53220 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 68 | 0.30 | 0.74 | 15 | empty |
Compared structures
- 2CIU · Structure of the IMS domain of the mitochondrial import protein Tim21 from S. cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
- P53220 · AlphaFold monomer V2.0 prediction for mitochondrial import inner membrane translocase… · a predicted model of the same protein · chain A against A, TM-score 0.87
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 P53220
- Elsewhere: RCSB PDB 2CIU · PDBe 2CIU · UniProt P53220
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