E. coli C-P lyase bound to a PhnK/PhnL dual ABC dimer and ADP + Pi
Resolution: 1.93 Å
EM Method: Single-particle
Fitted PDBs: 7z15
Q-score: 0.688
Amstrup SK, Ong SC, Sofos N, Karlsen JL, Skjerning RB, Boesen T, Enghild JJ, Hove-Jensen B, Brodersen DE
Nat Commun (2023) 14 pp. 1001-1001 [ Pubmed: 36813778 DOI: doi:10.1038/s41467-023-36604-y ]
- Adenosine-5'-triphosphate (507 Da, Ligand)
- Putative phosphonates utilization atp-binding protein phnk (31 kDa, Protein from Escherichia coli)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phni (38 kDa, Protein from Escherichia coli)
- Alpha-d-ribose-1,2-cyclic-phosphate-5-phosphate (292 Da, Ligand)
- Magnesium ion (24 Da, Ligand)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phng (16 kDa, Protein from Escherichia coli)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phnl (24 kDa, Protein from Escherichia coli)
- Adenosine-5'-diphosphate (427 Da, Ligand)
- Water (18 Da, Ligand)
- Alpha-d-ribose 1-methylphosphonate 5-phosphate c-p lyase (31 kDa, Protein from Escherichia coli)
- Phosphate ion (94 Da, Ligand)
- Zinc ion (65 Da, Ligand)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phnh (21 kDa, Protein from Escherichia coli)
- E. coli c-p lyase bound to a phnk/phnl dual abc dimer and adp + pi (327 kDa, Complex from Escherichia coli)
E. coli C-P lyase bound to PhnK/PhnL dual ABC dimer with AMPPNP and PhnK E171Q mutation
Resolution: 2.09 Å
EM Method: Single-particle
Fitted PDBs: 7z16
Q-score: 0.641
Amstrup SK, Ong SC, Sofos N, Karlsen JL, Skjerning RB, Boesen T, Enghild JJ, Hove-Jensen B, Brodersen DE
Nat Commun (2023) 14 pp. 1001-1001 [ Pubmed: 36813778 DOI: doi:10.1038/s41467-023-36604-y ]
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phnh (21 kDa, Protein from Escherichia coli)
- E. coli c-p lyase bound to phnk/phnl dual abc dimer with amppnp and phnk e171q mutation (327 kDa, Complex from Escherichia coli)
- Phosphoaminophosphonic acid-adenylate ester (506 Da, Ligand)
- Zinc ion (65 Da, Ligand)
- Water (18 Da, Ligand)
- Magnesium ion (24 Da, Ligand)
- Phosphate ion (94 Da, Ligand)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phnl (24 kDa, Protein from Escherichia coli)
- Alpha-d-ribose 1-methylphosphonate 5-phosphate c-p lyase (31 kDa, Protein from Escherichia coli)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phni (38 kDa, Protein from Escherichia coli)
- Phosphonate c-p lyase system protein phng (16 kDa, Protein from Escherichia coli)
- Putative phosphonates utilization atp-binding protein phnk (31 kDa, Protein from Escherichia coli)
E. coli C-P lyase bound to a PhnK ABC dimer in an open conformation
Resolution: 2.57 Å
EM Method: Single-particle
Fitted PDBs: 7z17
Q-score: 0.482
Amstrup SK, Ong SC, Sofos N, Karlsen JL, Skjerning RB, Boesen T, Enghild JJ, Hove-Jensen B, Brodersen DE
Nat Commun (2023) 14 pp. 1001-1001 [ Pubmed: 36813778 DOI: doi:10.1038/s41467-023-36604-y ]
- Putative phosphonates utilization atp-binding protein phnk (31 kDa, Protein from Escherichia coli)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phni (38 kDa, Protein from Escherichia coli)
- Alpha-d-ribose-1,2-cyclic-phosphate-5-phosphate (292 Da, Ligand)
- E. coli c-p lyase bound to a phnk abc dimer in an open conformation (277 kDa, Complex from Escherichia coli)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phng (16 kDa, Protein from Escherichia coli)
- Alpha-d-ribose 1-methylphosphonate 5-phosphate c-p lyase (31 kDa, Protein from Escherichia coli)
- Zinc ion (65 Da, Ligand)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phnh (21 kDa, Protein from Escherichia coli)
E. coli C-P lyase bound to a PhnK ABC dimer and ATP
Resolution: 1.98 Å
EM Method: Single-particle
Fitted PDBs: 7z18
Q-score: 0.666
Amstrup SK, Ong SC, Sofos N, Karlsen JL, Skjerning RB, Boesen T, Enghild JJ, Hove-Jensen B, Brodersen DE
Nat Commun (2023) 14 pp. 1001-1001 [ Pubmed: 36813778 DOI: doi:10.1038/s41467-023-36604-y ]
- Adenosine-5'-triphosphate (507 Da, Ligand)
- Putative phosphonates utilization atp-binding protein phnk (31 kDa, Protein from Escherichia coli)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phni (38 kDa, Protein from Escherichia coli)
- Alpha-d-ribose-1,2-cyclic-phosphate-5-phosphate (292 Da, Ligand)
- Magnesium ion (24 Da, Ligand)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phng (16 kDa, Protein from Escherichia coli)
- Water (18 Da, Ligand)
- Alpha-d-ribose 1-methylphosphonate 5-phosphate c-p lyase (31 kDa, Protein from Escherichia coli)
- E. coli c-p lyase bound to a phnk abc dimer and atp (277 kDa, Complex from Escherichia coli)
- Zinc ion (65 Da, Ligand)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phnh (21 kDa, Protein from Escherichia coli)
E. coli C-P lyase bound to a single PhnK ABC domain
Resolution: 2.57 Å
EM Method: Single-particle
Fitted PDBs: 7z19
Q-score: 0.586
Amstrup SK, Ong SC, Sofos N, Karlsen JL, Skjerning RB, Boesen T, Enghild JJ, Hove-Jensen B, Brodersen DE
Nat Commun (2023) 14 pp. 1001-1001 [ Pubmed: 36813778 DOI: doi:10.1038/s41467-023-36604-y ]
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phnh (21 kDa, Protein from Escherichia coli)
- Putative phosphonates utilization atp-binding protein phnk (28 kDa, Protein from Escherichia coli)
- Water (18 Da, Ligand)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phng (16 kDa, Protein from Escherichia coli)
- Alpha-d-ribose 1-methylphosphonate 5-phosphate c-p lyase (31 kDa, Protein from Escherichia coli)
- Phosphate ion (94 Da, Ligand)
- Zinc ion (65 Da, Ligand)
- E. coli c-p lyase bound to a single phnk abc domain (252 kDa, Complex from Escherichia coli)
- Alpha-d-ribose 1-methylphosphonate 5-triphosphate synthase subunit phni (38 kDa, Protein from Escherichia coli)