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AlphaFold monomer V2.0 prediction for glyceraldehyde-3-phosphate dehydrogenase (Q01651)

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

Accession: Q01651
Type: protein
Length: 334 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0x1e3895C6800c841C8828D11781a5f3Db2d1F9740
UniProt: Q01651

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	334	—	Q01651

Compared structures

8HRS · Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Corynebacterium… · an experimental structure of the same protein · chain A against B, TM-score 0.99
8HRP · Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Corynebacterium… · an experimental structure of the same protein · chain A against G, TM-score 0.99
8HRQ · Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Corynebacterium… · an experimental structure of the same protein · chain A against B, TM-score 0.99
8HRO · Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Corynebacterium… · an experimental structure of the same protein · chain A against B, TM-score 0.99
8HRR · Crystal structure of glyceraldehyde-3-phosphate dehydrogenase from Corynebacterium… · an experimental structure of the same protein · chain A against B, TM-score 0.99

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 Q01651
Elsewhere: UniProt Q01651 · AlphaFold DB Q01651

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