Research workbench

Human early B-cell factor 1 (EBF1) DNA-binding domain

Analyse Human early B-cell factor 1 (EBF1) DNA-binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LYR
Type: protein
Length: 211 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transcription factor COE1
UniProt: Q9UH73
Ligands: ZN, SO4, NH4
Pockets: 1 · best druggability 0.29

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transcription factor COE1	protein	211	12% helix, 39% strand	Q9UH73

Ligands and binding sites

ZN · Zinc ion · metal · chains A
SO4 · Sulfate ion · ion · chains A
NH4 · Ammonium ion · ion · 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	59	0.29	0.75	19	empty

Modifications

Observed in the structure: 7 modified (engineered).

Compared structures

3LYR · Human Early B-cell Factor 1 (EBF1) DNA-binding domain · the same entry in another collection · chain A against A, TM-score 1.00
Q9UH73 · AlphaFold monomer V2.0 prediction for transcription factor COE1 (Q9UH73) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 Q9UH73
Elsewhere: RCSB PDB 3LYR · PDBe 3LYR · UniProt Q9UH73

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