Research workbench
Structure analysis of the TOM1 gat domain reveals distinct ligand- specific conformational states
Analyse Structure analysis of the TOM1 gat domain reveals distinct ligand- specific… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2N9D
- Type
- protein
- Length
- 95 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Target of myb protein 1
- UniProt
- O60784
Structure
solution nmr · 1 distinct chain · 82% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Target of myb protein 1 | protein | 95 | 82% helix, 0% strand | O60784 |
Compared structures
- 2N9D · Structure analysis of the Tom1 GAT domain reveals distinct ligand-specific conformational… · the same entry in another collection · chain A against A, TM-score 1.00
- O60784 · AlphaFold monomer V2.0 prediction for target of myb protein 1 (O60784) · a predicted model of the same protein · chain A against A, TM-score 0.92
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 O60784
- Elsewhere: RCSB PDB 2N9D · PDBe 2N9D · UniProt O60784
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