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AlphaFold monomer V2.0 prediction for 2'-deoxynucleoside 5'-phosphate N-hydrolase 1 (O35820)

Analyse AlphaFold monomer V2.0 prediction for 2'-deoxynucleoside 5'-phosphate… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession: O35820
Type: protein
Length: 163 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x6f7d7ecD2D5477c07662463b2369E9953067f93b
UniProt: O35820

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	163	—	O35820

Compared structures

4P5D · Crystal structure of rat DNPH1 (rcl) with 6-naphthyl-purine-riboside- monophosphate · an experimental structure of the same protein · chain A against A, TM-score 0.86
4P5D · Crystal structure of rat DNPH1 (rcl) with 6-naphthyl-purine-riboside-monophosphate · an experimental structure of the same protein · chain A against A, TM-score 0.86
4KXL · Crystal structure of DNPH1 (rcl) with 6-cyclopentyl-AMP · an experimental structure of the same protein · chain A against D, TM-score 0.81
4KXL · Crystal structure of DNPH1 (RCL) with 6-CYCLOPENTYL-AMP · an experimental structure of the same protein · chain A against D, TM-score 0.81
4FYH · Crystal structure of rcl with phospho-triciribine · an experimental structure of the same protein · chain A against D, TM-score 0.80
4FYH · Crystal structure of rcl with phospho-triciribine · an experimental structure of the same protein · chain A against D, TM-score 0.80

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 O35820
Elsewhere: UniProt O35820 · AlphaFold DB O35820

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