MolNFT v1 · #177962 · protein

Crystal structure of the hlh-lz domain of human TFE3

7F09 · Transcription factor E3: “Crystal structure of the hlh-lz domain of human TFE3”. X-ray diffraction, 1 ligand (ZN), 1 pocket (best druggability 0.43). MolNFT v1 #177962 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7F09
Type: protein
Length: 274 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcription factor E3
UniProt: P19532
Ligands: ZN
Pockets: 1 · best druggability 0.43

Structure

x-ray diffraction · 4 distinct chains · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcription factor E3	protein	74	77% helix, 0% strand	P19532
B	Transcription factor E3	protein	68	79% helix, 0% strand	P19532
C	Transcription factor E3	protein	67	85% helix, 0% strand	P19532
D	Transcription factor E3	protein	65	86% helix, 0% strand	P19532

Ligands and binding sites

ZN · Zinc ion · metal · 6 copies · chains A, B, C, D
EDO · 1,2-ethanediol · additive · 6 copies · chains A, C, D, B

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	148	0.43	0.75	17	empty

Interfaces

3 interfaces between chains.

C–D · 1699 Å² buried · 13 hydrogen bonds · protein-protein
A–B · 1598 Å² buried · 8 hydrogen bonds · protein-protein
A–C · 364 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

7F09 · Crystal structure of the HLH-Lz domain of human TFE3 · the same entry in another collection · chain D against D, TM-score 1.00
P19532 · AlphaFold monomer V2.0 prediction for transcription factor E3 (P19532) · a predicted model of the same protein · chain C against A, TM-score 0.86

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 P19532
Elsewhere: RCSB PDB 7F09 · PDBe 7F09 · UniProt P19532

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