AlphaFold monomer V2.0 prediction for putative phosphonates utilization ATP-binding protein phnk (P16678)

Structure

1 distinct chain · 42% helix, 24% strand (DSSP).

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Compared structures

• 7Z19 · E. coli C-P lyase bound to a single PhnK ABC domain · an experimental structure of the same protein · chain A against I, TM-score 0.97
• 7Z19 · E. COLI C-P lyase bound to a single phnk ABC domain · an experimental structure of the same protein · chain A against I, TM-score 0.97
• 7Z17 · E. COLI C-P lyase bound to a phnk ABC dimer in an open conformation · an experimental structure of the same protein · chain A against J, TM-score 0.97
• 7Z17 · E. coli C-P lyase bound to a PhnK ABC dimer in an open conformation · an experimental structure of the same protein · chain A against J, TM-score 0.97
• 7Z16 · E. coli C-P lyase bound to PhnK/PhnL dual ABC dimer with AMPPNP and PhnK E171Q mutation · an experimental structure of the same protein · chain A against J, TM-score 0.94
• 7Z16 · E. COLI C-P lyase bound to PHNK/PHNL dual ABC dimer with amppnp and phnk E171Q mutation · an experimental structure of the same protein · chain A against J, TM-score 0.94
• 7Z18 · E. COLI C-P lyase bound to a phnk ABC dimer and ATP · an experimental structure of the same protein · chain A against I, TM-score 0.93
• 7Z18 · E. coli C-P lyase bound to a PhnK ABC dimer and ATP · an experimental structure of the same protein · chain A against I, TM-score 0.93

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 P16678
• Elsewhere: UniProt P16678 · AlphaFold DB P16678