MolNFT v1 · #146182 · protein

ETS1 in complex with synthetic srr mimic

6DA1 · Protein C-ets-1: “ETS1 in complex with synthetic srr mimic”. X-ray diffraction, 2 ligands (SO4, NH2), 3 pockets (best druggability 0.75). MolNFT v1 #146182 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6DA1
Type: protein
Length: 291 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein C-ets-1; Serine-rich region (srr) peptide
UniProt: P27577
Ligands: SO4, NH2
Pockets: 3 · best druggability 0.75

Structure

x-ray diffraction · 3 distinct chains · 46% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein C-ets-1	protein	137	49% helix, 9% strand	P27577
B	Protein C-ets-1	protein	138	49% helix, 9% strand	P27577
C	Serine-rich region (srr) peptide	protein	16	0% helix, 13% strand	—

Ligands and binding sites

SO4 · Sulfate ion · ion · 3 copies · chains A, B, C
NH2 · Amino group · ion · chains A, C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	717	0.75	0.80	58	SO4
2	147	0.59	0.83	29	empty
3	66	0.32	0.75	13	empty

Interfaces

3 interfaces between chains.

A–B · 1097 Å² buried · 20 hydrogen bonds · protein-protein
B–C · 799 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 191 Å² buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 6 modified (nonstandard, phosphorylation).

Compared structures

6DA1 · ETS1 in complex with synthetic SRR mimic · the same entry in another collection · chain A against A, TM-score 1.00
P27577 · AlphaFold monomer V2.0 prediction for protein C-ets-1 (P27577) · a predicted model of the same protein · chain A against A, TM-score 0.88

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 P27577
Elsewhere: RCSB PDB 6DA1 · PDBe 6DA1 · UniProt P27577

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