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NMR structure of an odin-SAM1 fragment

Analyse NMR structure of an odin-SAM1 fragment in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2MYQ
Type: protein
Length: 43 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ankyrin repeat and SAM domain-containing protein 1A
UniProt: Q92625
Ligands: ACE, NH2

Structure

solution nmr · 1 distinct chain · 81% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ankyrin repeat and SAM domain-containing protein 1A	protein	43	81% helix, 0% strand	Q92625

Ligands and binding sites

ACE · Acetyl group · ligand · chains A
NH2 · Amino group · ion · chains A

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

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

2MYQ · NMR structure of an Odin-Sam1 fragment · the same entry in another collection · chain A against A, TM-score 1.00
Q92625 · AlphaFold monomer V2.0 prediction for ankyrin repeat and SAM domain- containing protein… · a predicted model of the same protein · chain A against A, TM-score 0.61

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 Q92625
Elsewhere: RCSB PDB 2MYQ · PDBe 2MYQ · UniProt Q92625

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