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AlphaFold monomer V2.0 prediction for molybdopterin-synthase adenylyltransferase (P12282)

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

Accession: P12282
Type: protein
Length: 249 residues
Chains: 1
Collection: MolNFT v1 / AlphaFold
Contract: 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner: 0xd6DfE5bdDd44c5887584131C31217ED4556a11e4
UniProt: P12282

Structure

1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	249	—	P12282

Compared structures

1JWB · Structure of the Covalent Acyl-Adenylate Form of the MoeB-MoaD Protein Complex · an experimental structure of the same protein · chain A against B, TM-score 0.96
1JWB · Structure of the covalent acyl-adenylate form of the moeb-moad protein complex · an experimental structure of the same protein · chain A against B, TM-score 0.96
1JW9 · Structure of the Native MoeB-MoaD Protein Complex · an experimental structure of the same protein · chain A against B, TM-score 0.95
1JW9 · Structure of the native moeb-moad protein complex · an experimental structure of the same protein · chain A against B, TM-score 0.95
1JWA · Structure of the ATP-bound MoeB-MoaD Protein Complex · an experimental structure of the same protein · chain A against B, TM-score 0.86
1JWA · Structure of the ATP-bound moeb-moad protein complex · an experimental structure of the same protein · chain A against B, TM-score 0.86

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 P12282
Elsewhere: UniProt P12282 · AlphaFold DB P12282

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