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Crystal structure of TEAD3 in complex with CPD4

Analyse Crystal structure of TEAD3 in complex with CPD4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 8A0U
Type: protein
Length: 832 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcriptional enhancer factor tef-5
UniProt: P70210
Ligands: MYR, KMU, PO4
Pockets: 13 · best druggability 0.83

Structure

x-ray diffraction · 4 distinct chains · 17% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcriptional enhancer factor tef-5	protein	209	18% helix, 51% strand	P70210
B	Transcriptional enhancer factor tef-5	protein	209	17% helix, 51% strand	P70210
C	Transcriptional enhancer factor tef-5	protein	206	17% helix, 52% strand	P70210
D	Transcriptional enhancer factor tef-5	protein	208	18% helix, 51% strand	P70210

Ligands and binding sites

MYR · Myristic acid · ligand · 4 copies · chains A, B, C, D
KMU · 2-[(2~{S})-2-(aminomethyl)-5-chloranyl-2-phenyl-3~{H}-1-benzofuran-4-yl]benzamide · ligand · 4 copies · chains A, B, C, D
PO4 · Phosphate ion · ion · 8 copies · chains A, B, C, D

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

Pockets

13 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	197	0.83	0.97	37	MYR
2	198	0.83	0.96	35	MYR
3	157	0.82	0.97	32	MYR
4	521	0.80	0.86	67	MYR, PO4
5	1085	0.78	0.80	79	PO4

Interfaces

5 interfaces between chains.

A–C · 809 Å² buried · 17 hydrogen bonds · protein-protein
A–B · 680 Å² buried · 8 hydrogen bonds · protein-protein
C–D · 667 Å² buried · 7 hydrogen bonds · protein-protein
A–D · 229 Å² buried · 4 hydrogen bonds · protein-protein
B–C · 215 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 lipid (myristoylation).

Compared structures

8A0U · Crystal structure of TEAD3 in complex with CPD4 · the same entry in another collection · chain D against D, TM-score 1.00
P70210 · AlphaFold monomer V2.0 prediction for transcriptional enhancer factor tef-5 (P70210) · 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 P70210
Elsewhere: RCSB PDB 8A0U · PDBe 8A0U · UniProt P70210

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