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Crystal structure of human TBX5 in the DNA-free form

Analyse Crystal structure of human TBX5 in the DNA-free form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2X6U
Type: protein
Length: 176 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T-box transcription factor TBX5
UniProt: Q99593
Ligands: MG
Pockets: 1 · best druggability 0.36

Structure

x-ray diffraction · 1 distinct chain · 16% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	T-box transcription factor TBX5	protein	176	16% helix, 40% strand	Q99593

Ligands and binding sites

MG · Magnesium ion · metal · 4 copies · chains A
PE4 · 2-{2-[2-(2-{2-[2-(2-ethoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethanol · additive · 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	74	0.36	0.77	20	empty

Compared structures

2X6U · Crystal structure of human TBX5 in the DNA-free form · the same entry in another collection · chain A against A, TM-score 1.00
Q99593 · AlphaFold monomer V2.0 prediction for T-box transcription factor TBX5 (Q99593) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 Q99593
Elsewhere: RCSB PDB 2X6U · PDBe 2X6U · UniProt Q99593

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