Research workbench
Crystal structure of human brachyury G177D variant in complex with CSC027898502
Analyse Crystal structure of human brachyury G177D variant in complex with CSC027898502 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7ZK2
- 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
- IU4, PO4
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 39% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | T-box transcription factor T | protein | 171 | 16% helix, 39% strand | O15178 |
Ligands and binding sites
- IU4 · N-[4-(2-morpholin-4-yl-1,3-thiazol-4-yl) phenyl]ethanamide · ligand · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.44 | 0.82 | 24 | empty |
Compared structures
- 7ZK2 · Crystal Structure of human Brachyury G177D variant in complex with CSC027898502 · the same entry in another collection · chain A against A, TM-score 1.00
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 7ZK2 · PDBe 7ZK2 · UniProt O15178
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