Research workbench
Pandda analysis group deposition -- crystal structure of human brachyury in complex with Z1509882419
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
- 5QRW
- Type
- protein
- Length
- 171 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T-box transcription factor T
- UniProt
- O15178
- Ligands
- NYV, CD
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-box transcription factor T | protein | 171 | 16% helix, 38% strand | O15178 |
Ligands and binding sites
- NYV · 1-(propan-2-yl)-1H-imidazole-4-sulfonamide · ligand · 2 copies · chains A
- CD · Cadmium ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5QRW · 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 0.98
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 5QRW · PDBe 5QRW · UniProt O15178
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