Fluorine in PDB 8jwf: Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq

The binding sites of Fluorine atom in the Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq (pdb code 8jwf). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq, PDB code: 8jwf:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in the Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq within 5.0Å range: probe atom residue distance (Å) B Occ A:F1500 b:137.1 occ:1.00 FAE A:YMZ1500 0.0 137.1 1.0 CAZ A:YMZ1500 1.4 137.1 1.0 FAF A:YMZ1500 2.2 137.1 1.0 FAG A:YMZ1500 2.2 137.1 1.0 CAT A:YMZ1500 2.4 137.1 1.0 CAI A:YMZ1500 2.7 137.1 1.0 CAV A:YMZ1500 3.7 137.1 1.0 CG A:GLN1038 4.0 123.5 1.0 CAH A:YMZ1500 4.1 137.1 1.0 O A:SER1034 4.2 133.2 1.0 NAP A:YMZ1500 4.2 137.1 1.0 NH2 A:ARG950 4.2 147.9 1.0 CAU A:YMZ1500 4.8 137.1 1.0 CB A:GLN1038 4.9 123.5 1.0 CAJ A:YMZ1500 5.0 137.1 1.0

Fluorine binding site 2 out of 6 in the Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq within 5.0Å range: probe atom residue distance (Å) B Occ A:F1500 b:137.1 occ:1.00 FAF A:YMZ1500 0.0 137.1 1.0 CAZ A:YMZ1500 1.4 137.1 1.0 FAG A:YMZ1500 2.2 137.1 1.0 FAE A:YMZ1500 2.2 137.1 1.0 CAT A:YMZ1500 2.4 137.1 1.0 NAP A:YMZ1500 2.9 137.1 1.0 CAV A:YMZ1500 3.0 137.1 1.0 CG A:GLN1038 3.3 123.5 1.0 CAI A:YMZ1500 3.4 137.1 1.0 CB A:GLN1038 3.7 123.5 1.0 CAR A:YMZ1500 4.1 137.1 1.0 FAD A:YMZ1500 4.2 137.1 1.0 CAU A:YMZ1500 4.3 137.1 1.0 CAH A:YMZ1500 4.6 137.1 1.0 CD A:GLN1038 4.6 123.5 1.0 CAY A:YMZ1500 4.8 137.1 1.0 N A:GLN1038 4.9 123.5 1.0 CA A:GLN1038 4.9 123.5 1.0 CAJ A:YMZ1500 4.9 137.1 1.0

Fluorine binding site 3 out of 6 in the Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq within 5.0Å range: probe atom residue distance (Å) B Occ A:F1500 b:137.1 occ:1.00 FAG A:YMZ1500 0.0 137.1 1.0 CAZ A:YMZ1500 1.4 137.1 1.0 FAF A:YMZ1500 2.2 137.1 1.0 FAE A:YMZ1500 2.2 137.1 1.0 CAT A:YMZ1500 2.4 137.1 1.0 NAP A:YMZ1500 2.9 137.1 1.0 CAV A:YMZ1500 3.0 137.1 1.0 CAI A:YMZ1500 3.4 137.1 1.0 CAR A:YMZ1500 4.2 137.1 1.0 CAU A:YMZ1500 4.3 137.1 1.0 CAH A:YMZ1500 4.6 137.1 1.0 FAD A:YMZ1500 4.7 137.1 1.0 FAC A:YMZ1500 4.8 137.1 1.0 CAY A:YMZ1500 4.8 137.1 1.0 CAJ A:YMZ1500 4.9 137.1 1.0

Fluorine binding site 4 out of 6 in the Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq within 5.0Å range: probe atom residue distance (Å) B Occ A:F1500 b:137.1 occ:1.00 FAC A:YMZ1500 0.0 137.1 1.0 CAY A:YMZ1500 1.4 137.1 1.0 FAB A:YMZ1500 2.2 137.1 1.0 FAD A:YMZ1500 2.2 137.1 1.0 CAR A:YMZ1500 2.4 137.1 1.0 NAP A:YMZ1500 3.1 137.1 1.0 CAK A:YMZ1500 3.3 137.1 1.0 CD1 A:LEU71 4.2 109.3 1.0 CAV A:YMZ1500 4.3 137.1 1.0 CAS A:YMZ1500 4.5 137.1 1.0 CE A:MET332 4.6 113.5 1.0 FAG A:YMZ1500 4.8 137.1 1.0 CAU A:YMZ1500 4.9 137.1 1.0

Fluorine binding site 5 out of 6 in the Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq within 5.0Å range: probe atom residue distance (Å) B Occ A:F1500 b:137.1 occ:1.00 FAD A:YMZ1500 0.0 137.1 1.0 CAY A:YMZ1500 1.4 137.1 1.0 FAB A:YMZ1500 2.2 137.1 1.0 FAC A:YMZ1500 2.2 137.1 1.0 CAR A:YMZ1500 2.4 137.1 1.0 NAP A:YMZ1500 2.8 137.1 1.0 CAK A:YMZ1500 3.6 137.1 1.0 CAV A:YMZ1500 4.1 137.1 1.0 FAF A:YMZ1500 4.2 137.1 1.0 CD2 A:LEU71 4.3 109.3 1.0 CD1 A:LEU71 4.4 109.3 1.0 CAS A:YMZ1500 4.7 137.1 1.0 FAG A:YMZ1500 4.7 137.1 1.0 CAZ A:YMZ1500 4.9 137.1 1.0 CAU A:YMZ1500 4.9 137.1 1.0

Fluorine binding site 6 out of 6 in the Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of Cryo-Em Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 with H1 Helix in Complex with Mfq within 5.0Å range: probe atom residue distance (Å) B Occ A:F1500 b:137.1 occ:1.00 FAB A:YMZ1500 0.0 137.1 1.0 CAY A:YMZ1500 1.4 137.1 1.0 FAC A:YMZ1500 2.2 137.1 1.0 FAD A:YMZ1500 2.2 137.1 1.0 CAR A:YMZ1500 2.4 137.1 1.0 CAK A:YMZ1500 2.7 137.1 1.0 NAP A:YMZ1500 3.6 137.1 1.0 CAS A:YMZ1500 4.1 137.1 1.0 CD1 A:ILE328 4.1 111.8 1.0 CG2 A:ILE328 4.5 111.8 1.0 CAV A:YMZ1500 4.7 137.1 1.0 CG1 A:ILE328 4.7 111.8 1.0 CD1 A:LEU71 4.7 109.3 1.0 CAU A:YMZ1500 4.9 137.1 1.0 CAW A:YMZ1500 4.9 137.1 1.0

K.Si, X.He, L.Chen, A.Zhang, C.Guo, M.Li. The Structure of Plasmodium Falciparum Multidrug Resistance Protein 1 Reveals An N-Terminal Regulatory Domain. Proc.Natl.Acad.Sci.Usa V. 120 05120 2023.
ISSN: ESSN 1091-6490
PubMed: 37527341
DOI: 10.1073/PNAS.2219905120