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Pandda analysis group deposition -- crystal structure of human brachyury G177D variant in complex with Z2856434778

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: 5QSA
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: K2P
Pockets: 1 · best druggability 0.42

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T-box transcription factor T	protein	171	17% helix, 39% strand	O15178

Ligands and binding sites

K2P · 2-(trifluoromethoxy)benzoic acid · ligand · 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.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	58	0.42	0.82	23	empty

Compared structures

5QSA · 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 5QSA · PDBe 5QSA · UniProt O15178

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