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Crystal structure of the ets domain of human ETS2 in complex with DNA

Analyse Crystal structure of the ets domain of human ETS2 in complex with DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4BQA
Type: protein + DNA
Length: 361 residues
Chains: 9
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein C-ets-2; 5'-D(*AP*CP*CP*GP*GP*AP*AP*GP*TP*GP)-3'…
UniProt: P15036
Pockets: 6 · best druggability 0.58

Structure

x-ray diffraction · 5 distinct chains · 44% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein C-ets-2	protein	132	43% helix, 9% strand	P15036
B, E, H	5'-D(APCPCPGPGPAPAPGPTPGP)-3'	dna	10	—	—
C, F, I	5'-D(CPAPCPTPTPCPCPGPGPTP)-3'	dna	10	—	—
D	Protein C-ets-2	protein	84	42% helix, 14% strand	P15036
G	Protein C-ets-2	protein	85	46% helix, 14% strand	P15036

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	354	0.58	0.77	27	empty
2	89	0.36	0.76	14	empty
3	73	0.36	0.77	14	empty
4	59	0.35	0.78	19	empty
5	59	0.30	0.75	15	empty

Interfaces

21 interfaces between chains.

A–C · 547 Å² buried · 10 hydrogen bonds · protein-nucleic
D–F · 472 Å² buried · 7 hydrogen bonds · protein-nucleic
G–I · 462 Å² buried · 8 hydrogen bonds · protein-nucleic
E–F · 457 Å² buried · 54 hydrogen bonds · nucleic-nucleic
H–I · 455 Å² buried · 48 hydrogen bonds · nucleic-nucleic

Compared structures

4BQA · Crystal structure of the ETS domain of human ETS2 in complex with DNA · the same entry in another collection · chain I against I, TM-score 1.00
P15036 · AlphaFold monomer V2.0 prediction for protein C-ets-2 (P15036) · a predicted model of the same protein · chain G against A, TM-score 0.97

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 P15036
Elsewhere: RCSB PDB 4BQA · PDBe 4BQA · UniProt P15036

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