Fluorine in PDB 8iok: Crystal Structure of Athppd-CLJ507 Complex

All present enzymatic activity of Crystal Structure of Athppd-CLJ507 Complex:
1.13.11.27;

The structure of Crystal Structure of Athppd-CLJ507 Complex, PDB code: 8iok was solved by J.Dong, G.-F.Yang, H.-Y.Lin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.55 / 1.99
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	77.67, 84.251, 64.191, 90, 100.53, 90
R / Rfree (%)	23.6 / 28

The structure of Crystal Structure of Athppd-CLJ507 Complex also contains other interesting chemical elements:

Cobalt

(Co)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of Athppd-CLJ507 Complex (pdb code 8iok). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Crystal Structure of Athppd-CLJ507 Complex, PDB code: 8iok:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Athppd-CLJ507 Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Crystal Structure of Athppd-CLJ507 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F502 b:80.2 occ:1.00 F26 A:SYI502 0.0 80.2 1.0 C25 A:SYI502 1.4 80.8 1.0 F27 A:SYI502 2.2 88.7 1.0 F28 A:SYI502 2.3 83.4 1.0 C6 A:SYI502 2.3 82.5 1.0 C1 A:SYI502 3.1 78.2 1.0 CZ A:PHE392 3.2 61.3 1.0 N5 A:SYI502 3.3 90.6 1.0 C7 A:SYI502 3.3 72.1 1.0 CE2 A:PHE392 3.4 63.4 1.0 CE1 A:HIS308 3.5 63.8 1.0 O08 A:SYI502 3.5 68.5 1.0 CE1 A:PHE381 3.6 72.8 1.0 ND1 A:HIS308 3.6 58.2 1.0 CZ A:PHE381 3.9 78.4 1.0 NE2 A:HIS308 4.0 60.6 1.0 N9 A:SYI502 4.1 72.8 1.0 OE1 A:GLN307 4.2 64.5 1.0 CD1 A:PHE381 4.2 71.0 1.0 C16 A:SYI502 4.2 89.7 1.0 CG A:HIS308 4.3 61.3 1.0 C17 A:SYI502 4.4 89.0 1.0 C2 A:SYI502 4.4 82.8 1.0 CD2 A:HIS308 4.5 59.1 1.0 C4 A:SYI502 4.5 90.4 1.0 CE1 A:PHE392 4.5 59.1 1.0 CD A:GLN307 4.7 65.3 1.0 CE2 A:PHE381 4.7 80.0 1.0 CD2 A:PHE392 4.8 58.8 1.0 NE2 A:GLN307 4.8 70.0 1.0 CG A:PHE381 5.0 66.9 1.0 CO A:CO501 5.0 68.6 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Athppd-CLJ507 Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Crystal Structure of Athppd-CLJ507 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F502 b:88.7 occ:1.00 F27 A:SYI502 0.0 88.7 1.0 C25 A:SYI502 1.4 80.8 1.0 F26 A:SYI502 2.2 80.2 1.0 F28 A:SYI502 2.3 83.4 1.0 C6 A:SYI502 2.4 82.5 1.0 N5 A:SYI502 2.7 90.6 1.0 C1 A:SYI502 3.8 78.2 1.0 C17 A:SYI502 4.0 89.0 1.0 NE2 A:GLN307 4.0 70.0 1.0 CZ A:PHE392 4.0 61.3 1.0 NE2 A:GLN293 4.1 83.0 1.0 C16 A:SYI502 4.1 89.7 1.0 OE1 A:GLN307 4.1 64.5 1.0 C4 A:SYI502 4.2 90.4 1.0 CD A:GLN307 4.4 65.3 1.0 C7 A:SYI502 4.5 72.1 1.0 CD2 A:LEU265 4.6 82.6 1.0 CE2 A:PHE392 4.8 63.4 1.0 N9 A:SYI502 4.8 72.8 1.0 CE1 A:PHE392 4.9 59.1 1.0 CE1 A:HIS308 5.0 63.8 1.0 N14 A:SYI502 5.0 96.8 1.0 C2 A:SYI502 5.0 82.8 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Athppd-CLJ507 Complex


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Crystal Structure of Athppd-CLJ507 Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:F502 b:83.4 occ:1.00 F28 A:SYI502 0.0 83.4 1.0 C25 A:SYI502 1.4 80.8 1.0 F27 A:SYI502 2.3 88.7 1.0 F26 A:SYI502 2.3 80.2 1.0 C6 A:SYI502 2.4 82.5 1.0 N9 A:SYI502 2.8 72.8 1.0 C7 A:SYI502 2.9 72.1 1.0 C1 A:SYI502 3.0 78.2 1.0 CE1 A:HIS308 3.4 63.8 1.0 O08 A:SYI502 3.6 68.5 1.0 OE1 A:GLN307 3.6 64.5 1.0 N5 A:SYI502 3.6 90.6 1.0 C19 A:SYI502 3.7 68.6 1.0 ND1 A:HIS308 4.0 58.2 1.0 ND2 A:ASN282 4.2 66.2 1.0 NE2 A:HIS308 4.3 60.6 1.0 N23 A:SYI502 4.4 71.4 1.0 C2 A:SYI502 4.4 82.8 1.0 CD A:GLN307 4.5 65.3 1.0 N20 A:SYI502 4.5 64.4 1.0 C24 A:SYI502 4.6 69.4 1.0 NE2 A:GLN307 4.6 70.0 1.0 CD2 A:LEU265 4.8 82.6 1.0 C4 A:SYI502 4.9 90.4 1.0 CZ A:PHE392 4.9 61.3 1.0

J.Dong, G.-F.Yang, H.-Y.Lin. Crystal Structure of Human Hppd-Ntbc Complex To Be Published.