Research workbench

Engineering protein stability with atomic precision in a monomeric miniprotein

Analyse Engineering protein stability with atomic precision in a monomeric miniprotein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5LO3
Type: protein
Length: 34 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ppaome
Ligands: ACE, NH2

Structure

solution nmr · 1 distinct chain · 59% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ppaome	protein	34	59% helix, 0% strand	—

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: 3 modified, 1 covalent (nonstandard, covalent ligand).

Compared structures

5LO3 · Engineering protein stability with atomic precision in a monomeric miniprotein · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Elsewhere: RCSB PDB 5LO3 · PDBe 5LO3

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