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Structural characteristics for biological activity of heat-stable enterotoxin produced by enterotoxigenic escherichia COLI: X-ray crystallography of weakly toxic and nontoxic analogs

Analyse Structural characteristics for biological activity of heat-stable enterotoxin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ETL
Type: protein
Length: 12 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 5-beta-mercaptopropionate heat-stable enterotoxin
UniProt: P01559
Ligands: MPR

Structure

x-ray diffraction · 1 distinct chain · 0% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	5-beta-mercaptopropionate heat-stable enterotoxin	protein	12	0% helix, 0% strand	P01559

Ligands and binding sites

MPR · 2-mercapto-propion aldehyde · ligand · chains A

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

Modifications

Observed in the structure: 2 covalent, 2 disulfide (covalent ligand, disulfide).

Compared structures

1ETL · Structural characteristics for biological activity of heat-stable enterotoxin produced by… · the same entry in another collection · chain A against A, TM-score 1.00
P01559 · AlphaFold monomer V2.0 prediction for heat-stable enterotoxin st- IA/ST-P (P01559) · a predicted model of the same protein · chain A against A, TM-score 0.35

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P01559
Elsewhere: RCSB PDB 1ETL · PDBe 1ETL · UniProt P01559

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