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Solution structure of the mynd domain from human AML1-eto

Analyse Solution structure of the mynd domain from human AML1-eto in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2OD1
Type: protein
Length: 50 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein CBFA2T1
UniProt: Q06455
Ligands: ZN

Structure

solution nmr · 1 distinct chain · 22% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein CBFA2T1	protein	50	22% helix, 8% strand	Q06455

Ligands and binding sites

ZN · Zinc ion · metal · 2 copies · chains A

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

Compared structures

2OD1 · Solution structure of the MYND domain from human AML1-ETO · the same entry in another collection · chain A against A, TM-score 1.00
Q06455 · AlphaFold monomer V2.0 prediction for protein CBFA2T1 (Q06455) · a predicted model of the same protein · chain A against A, TM-score 0.74

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 Q06455
Elsewhere: RCSB PDB 2OD1 · PDBe 2OD1 · UniProt Q06455

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