MolNFT v1 · #87084 · protein + DNA

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

4BQA · Protein C-ets-2: “Crystal structure of the ets domain of human ETS2 in complex with DNA”. X-ray diffraction, 6 pockets (best druggability 0.58). MolNFT v1 #87084 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

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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