Research workbench

Crystal structure of the superantigen spe-H from streptococcus pyogenes

Analyse Crystal structure of the superantigen spe-H from streptococcus pyogenes in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ET9
Type: protein
Length: 195 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Superantigen spe-H
UniProt: P0C0I6

Structure

x-ray diffraction · 1 distinct chain · 23% helix, 38% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Superantigen spe-H	protein	195	23% helix, 38% strand	P0C0I6

Compared structures

1ET9 · Crystal structure of the superantigen spe-H from streptococcus pyogenes · the same entry in another collection · chain A against A, TM-score 1.00
P0C0I6 · AlphaFold monomer V2.0 prediction for exotoxin type H (P0C0I6) · a predicted model of the same protein · 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
Every structure of UniProt P0C0I6
Elsewhere: RCSB PDB 1ET9 · PDBe 1ET9 · UniProt P0C0I6

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.