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Crystal structure of the DNA binding ets domain of human protein fev

Analyse Crystal structure of the DNA binding ets domain of human protein fev in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2YPR
Type: protein
Length: 188 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein fev
UniProt: Q99581
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein fev	protein	96	45% helix, 13% strand	Q99581
B	Protein fev	protein	92	45% helix, 13% strand	Q99581

Ligands and binding sites

GOL · Glycerol · 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	79	0.37	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 829 Å² buried · 3 hydrogen bonds · protein-protein

Compared structures

2YPR · Crystal structure of the DNA binding ETS domain of human protein FEV · the same entry in another collection · chain A against A, TM-score 1.00
Q99581 · AlphaFold monomer V2.0 prediction for protein fev (Q99581) · a predicted model of the same protein · chain B against A, TM-score 0.95

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 Q99581
Elsewhere: RCSB PDB 2YPR · PDBe 2YPR · UniProt Q99581

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