MolNFT v2 · #195330 · protein
The ubiquitin-associated domain of human thirty-eight negative kinase 1, flexibly fused to the 1TEL crystallization chaperone via a 2-glycine linker and crystallized at low protein concentration
7TDY: “The ubiquitin-associated domain of human thirty-eight negative kinase 1, flexibly fused to the 1TEL…”. X-ray diffraction at 1.53. MolNFT v2 #195330 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7TDY
- Type
- protein
- Length
- 147 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.53
- Source
- Homo sapiens
- UniProt
- P41212, Q13470
Structure
x-ray diffraction · resolution 1.53 · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 147 | — | P41212, Q13470 |
Ligands and binding sites
- FMT · Formic acid · additive · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- Q13470 · AlphaFold monomer V2.0 prediction for non-receptor tyrosine-protein kinase TNK1 (Q13470) · a predicted model of the same protein · chain A against A, TM-score 0.52
- P41212 · AlphaFold monomer V2.0 prediction for transcription factor ETV6 (P41212) · a predicted model of the same protein · chain A against A, TM-score 0.48
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 P41212
- Every structure of UniProt Q13470
- Elsewhere: RCSB PDB 7TDY · PDBe 7TDY · UniProt P41212 · UniProt Q13470
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