Research workbench
PanDDA analysis group deposition -- Crystal Structure of human Brachyury in complex with Z416341642
Analyse PanDDA analysis group deposition -- Crystal Structure of human Brachyury in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5QRJ
- Type
- protein
- Length
- 171 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.81
- Source
- Homo sapiens
- Molecule
- T-box transcription factor T
- UniProt
- O15178
- Ligands
- NWP, CD
Structure
x-ray diffraction · resolution 1.81 · 1 distinct chain · 16% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-box transcription factor T | protein | 171 | 16% helix, 37% strand | O15178 |
Ligands and binding sites
- NWP · (2R)-N,2-dimethyl-N-(propan-2-yl)morpholine-4-sulfonamide · ligand · chains A
- CD · Cadmium ion · metal · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5QRJ · Pandda analysis group deposition -- crystal structure of human brachyury in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- O15178 · AlphaFold monomer V2.0 prediction for T-box transcription factor T (O15178) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 O15178
- Elsewhere: RCSB PDB 5QRJ · PDBe 5QRJ · UniProt O15178
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