Research workbench
Pandda analysis group deposition -- crystal structure of human brachyury G177D variant in complex with Z2856434903
Analyse Pandda analysis group deposition -- crystal structure of human brachyury G177D… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5QSG
- 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
- O1A
Structure
x-ray diffraction · 1 distinct chain · 15% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-box transcription factor T | protein | 171 | 15% helix, 39% strand | O15178 |
Ligands and binding sites
- O1A · N-[4-(4-methylpiperazin-1-yl)phenyl]acetamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5QSG · PanDDA analysis group deposition -- Crystal Structure of human Brachyury G177D variant in… · 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 5QSG · PDBe 5QSG · UniProt O15178
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