MolNFT v1 · #147044 · protein

AlphaFold monomer V2.0 prediction for glutathione hydrolase proenzyme (P18956)

P18956: “AlphaFold monomer V2.0 prediction for glutathione hydrolase proenzyme (P18956)”. MolNFT v1 #147044 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

Accession: P18956
Type: protein
Length: 580 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
UniProt: P18956

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	580	—	P18956

Compared structures

2E0W · T391A precursor mutant protein of gamma-Glutamyltranspeptidase from Escherichia coli · an experimental structure of the same protein · chain A against B, TM-score 0.84
2E0W · T391A precursor mutant protein of gamma-glutamyltranspeptidase from escherichia COLI · an experimental structure of the same protein · chain A against B, TM-score 0.84
2DBU · Crystal structure of gamma-glutamyltranspeptidase from escherichia COLI · an experimental structure of the same protein · chain A against A, TM-score 0.60
2DBU · Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli · an experimental structure of the same protein · chain A against A, TM-score 0.60
2DBW · Crystal Structure of Gamma-glutamyltranspeptidase from Escherichia coli Acyl-Enzyme… · an experimental structure of the same protein · chain A against A, TM-score 0.60
2DBW · Crystal structure of gamma-glutamyltranspeptidase from escherichia COLI acyl-enzyme… · an experimental structure of the same protein · chain A against A, TM-score 0.60

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 P18956
Elsewhere: UniProt P18956 · AlphaFold DB P18956

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