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NMR structure of the redox switch domain of the E. COLI HSP33

Analyse NMR structure of the redox switch domain of the E. COLI HSP33 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XJH
Type: protein
Length: 62 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 33 kda chaperonin
UniProt: P0A6Y5
Ligands: ZN

Structure

solution nmr · 1 distinct chain · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	33 kda chaperonin	protein	62	44% helix, 16% strand	P0A6Y5

Ligands and binding sites

ZN · Zinc ion · metal · chains A

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

Compared structures

1XJH · NMR structure of the redox switch domain of the E. coli Hsp33 · the same entry in another collection · chain A against A, TM-score 1.00
P0A6Y5 · AlphaFold monomer V2.0 prediction for 33 kda chaperonin (P0A6Y5) · a predicted model of the same protein · chain A against A, TM-score 0.69

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 P0A6Y5
Elsewhere: RCSB PDB 1XJH · PDBe 1XJH · UniProt P0A6Y5

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