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The crystal structure of TLE4-TLI4 complex

Analyse The crystal structure of TLE4-TLI4 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4R1D
Type: protein
Length: 818 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Uncharacterized protein
UniProt: Q9I3K2, Q9I3K3
Ligands: CA
Pockets: 11 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Uncharacterized protein	protein	517	38% helix, 14% strand	Q9I3K2
B	Uncharacterized protein	protein	301	20% helix, 42% strand	Q9I3K3

Ligands and binding sites

CA · Calcium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

11 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	760	0.79	0.83	74	empty
2	220	0.76	0.90	36	empty
3	109	0.63	0.88	21	empty
4	108	0.49	0.81	16	empty
5	190	0.48	0.76	31	empty

Interfaces

1 interface between chains.

A–B · 2870 Å² buried · 38 hydrogen bonds · protein-protein

Compared structures

4R1D · The crystal structure of Tle4-Tli4 complex · 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 Q9I3K2
Every structure of UniProt Q9I3K3
Elsewhere: RCSB PDB 4R1D · PDBe 4R1D · UniProt Q9I3K2 · UniProt Q9I3K3

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