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UniProt P16686

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH (P16686)

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH (UniProt P16686), EC 2.7.8.37: 10 experimental structures and 1 predicted model on GenesisL1, 23 pockets. Binding sites, druggability and experiment against…

UniProt
P16686
Protein
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH
EC
2.7.8.37
Experimental structures
10
Predicted models
1
Pockets
23 · 6 records with a druggable one

Structures

11 records of P16686 in the MolNFT archive: 10 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
2FSUCrystal Structure of the PhnH Protein from Escherichia Colix-ray diffractionA——
2FSUCrystal structure of the phnh protein from escherichia COLIx-ray diffractionA——
4XB6Structure of the E. COLI C-P lyase core complexx-ray diffractionB, F——
7Z15E. coli C-P lyase bound to a PhnK/PhnL dual ABC dimer and ADP + Pielectron microscopyB, F——
7Z15E. COLI C-P lyase bound to a PHNK/PHNL dual ABC dimer and ADP + pielectron microscopyB, F—3 (best 0.77)
7Z16E. COLI C-P lyase bound to PHNK/PHNL dual ABC dimer with amppnp and phnk E171Q mutationelectron microscopyB, F—2 (best 0.78)
7Z17E. coli C-P lyase bound to a PhnK ABC dimer in an open conformationelectron microscopyB, F—5 (best 0.77)
7Z17E. COLI C-P lyase bound to a phnk ABC dimer in an open conformationelectron microscopyB, F—5 (best 0.77)
7Z18E. coli C-P lyase bound to a PhnK ABC dimer and ATPelectron microscopyB, F—4 (best 0.77)
7Z18E. COLI C-P lyase bound to a phnk ABC dimer and ATPelectron microscopyB, F—4 (best 0.77)
P16686AlphaFold monomer V2.0 prediction for alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase…predictedA——

Experiment against prediction

Elsewhere

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