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ETS1 in complex with synthetic srr mimic

Analyse ETS1 in complex with synthetic srr mimic in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6DAT
Type: protein
Length: 572 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P27577
Ligands: SO4, NH2

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	—	protein	135	—	P27577
E, F	—	protein	16	—	—

Ligands and binding sites

SO4 · Sulfate ion · ion · 9 copies · chains A, B, C, D
NH2 · Amino group · ion · 2 copies · chains B, E, D, F

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

Compared structures

6DAT · ETS1 in complex with synthetic SRR mimic · the same entry in another collection · chain F against F, 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 6DAT · PDBe 6DAT · UniProt P27577

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