Fluorine in PDB 4qjx: Crystal Structure of Human Carbonic Anhydrase Isozyme XIII with Inhibitor

All present enzymatic activity of Crystal Structure of Human Carbonic Anhydrase Isozyme XIII with Inhibitor:
4.2.1.1;

The structure of Crystal Structure of Human Carbonic Anhydrase Isozyme XIII with Inhibitor, PDB code: 4qjx was solved by A.Smirnov, E.Manakova, S.Grazulis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	53.53 / 1.95
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	56.822, 56.822, 159.608, 90.00, 90.00, 90.00
R / Rfree (%)	19 / 23.7

The structure of Crystal Structure of Human Carbonic Anhydrase Isozyme XIII with Inhibitor also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Fluorine atom in the Crystal Structure of Human Carbonic Anhydrase Isozyme XIII with Inhibitor (pdb code 4qjx). 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 Human Carbonic Anhydrase Isozyme XIII with Inhibitor, PDB code: 4qjx:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Crystal Structure of Human Carbonic Anhydrase Isozyme XIII with Inhibitor


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 Human Carbonic Anhydrase Isozyme XIII with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F304 b:22.4 occ:1.00 F27 A:WWO304 0.0 22.4 1.0 C5 A:WWO304 1.3 22.7 1.0 C4 A:WWO304 2.4 22.5 1.0 C6 A:WWO304 2.4 25.1 1.0 N26 A:WWO304 2.8 27.1 1.0 C14 A:WWO304 3.0 27.1 1.0 S7 A:WWO304 3.0 23.3 1.0 O8 A:WWO304 3.2 23.2 1.0 O9 A:WWO304 3.4 23.1 1.0 C3 A:WWO304 3.6 24.4 1.0 C1 A:WWO304 3.6 27.1 1.0 C20 A:WWO304 3.7 31.2 1.0 CD2 A:LEU200 3.7 12.5 1.0 C15 A:WWO304 3.8 29.8 1.0 C2 A:WWO304 4.1 26.3 1.0 CG2 A:VAL202 4.2 13.0 1.0 CD1 A:LEU200 4.2 13.0 1.0 CG A:LEU200 4.3 12.7 1.0 CB A:LEU200 4.3 12.7 1.0 CE1 A:HIS96 4.7 13.5 1.0 N10 A:WWO304 4.7 17.9 1.0 F12 A:WWO304 4.8 25.5 1.0 C19 A:WWO304 5.0 30.8 1.0

Fluorine binding site 2 out of 3 in the Crystal Structure of Human Carbonic Anhydrase Isozyme XIII with Inhibitor


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 Human Carbonic Anhydrase Isozyme XIII with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F304 b:25.5 occ:1.00 F12 A:WWO304 0.0 25.5 1.0 C3 A:WWO304 1.3 24.4 1.0 C2 A:WWO304 2.3 26.3 1.0 C4 A:WWO304 2.5 22.5 1.0 F13 A:WWO304 2.5 25.0 1.0 N10 A:WWO304 2.7 17.9 1.0 NE2 A:HIS96 2.8 11.4 1.0 ZN A:ZN301 2.9 12.9 1.0 CE1 A:HIS98 3.0 10.6 1.0 NE2 A:HIS98 3.1 11.0 1.0 S7 A:WWO304 3.2 23.3 1.0 CD2 A:HIS96 3.2 12.5 1.0 O A:HOH546 3.4 23.1 1.0 CE1 A:HIS96 3.5 13.5 1.0 C1 A:WWO304 3.6 27.1 1.0 CG1 A:VAL202 3.7 11.2 1.0 C5 A:WWO304 3.7 22.7 1.0 CG A:HIS96 4.1 12.9 1.0 C6 A:WWO304 4.2 25.1 1.0 ND1 A:HIS96 4.2 12.1 1.0 CG2 A:VAL202 4.3 13.0 1.0 O9 A:WWO304 4.3 23.1 1.0 ND1 A:HIS98 4.3 10.7 1.0 CD2 A:HIS98 4.3 10.1 1.0 O8 A:WWO304 4.4 23.2 1.0 OG1 A:THR201 4.4 10.4 1.0 CB A:VAL202 4.6 11.8 1.0 F27 A:WWO304 4.8 22.4 1.0 CG A:HIS98 4.9 10.2 1.0 ND1 A:HIS121 5.0 12.0 1.0

Fluorine binding site 3 out of 3 in the Crystal Structure of Human Carbonic Anhydrase Isozyme XIII with Inhibitor


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 Human Carbonic Anhydrase Isozyme XIII with Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:F304 b:25.0 occ:1.00 F13 A:WWO304 0.0 25.0 1.0 C2 A:WWO304 1.4 26.3 1.0 C3 A:WWO304 2.3 24.4 1.0 C1 A:WWO304 2.4 27.1 1.0 F12 A:WWO304 2.5 25.5 1.0 O22 A:WWO304 2.8 32.8 1.0 O A:HOH546 3.0 23.1 1.0 S11 A:WWO304 3.1 29.9 1.0 C4 A:WWO304 3.7 22.5 1.0 O A:HOH594 3.7 25.9 1.0 C6 A:WWO304 3.7 25.1 1.0 CG1 A:VAL202 4.0 11.2 1.0 CB A:HIS66 4.0 15.5 1.0 C21 A:WWO304 4.1 33.4 1.0 C5 A:WWO304 4.1 22.7 1.0 CB A:SER67 4.3 13.7 1.0 CG2 A:VAL202 4.3 13.0 1.0 O23 A:WWO304 4.4 37.6 1.0 CD2 A:HIS96 4.4 12.5 1.0 NE2 A:HIS96 4.5 11.4 1.0 CG A:HIS96 4.5 12.9 1.0 OG A:SER64 4.5 15.2 1.0 ND2 A:ASN69 4.7 22.6 0.5 C A:HIS66 4.7 13.9 1.0 ND1 A:HIS96 4.7 12.1 1.0 CE1 A:HIS96 4.8 13.5 1.0 CB A:VAL202 4.8 11.8 1.0 O A:HIS66 4.8 14.0 1.0 CE1 A:HIS98 4.8 10.6 1.0 N A:SER67 4.9 14.0 1.0 N26 A:WWO304 4.9 27.1 1.0 CG A:HIS66 5.0 18.5 1.0

V.Dudutiene, A.Zubriene, A.Smirnov, D.D.Timm, J.Smirnoviene, J.Kazokaite, V.Michailoviene, A.Zaksauskas, E.Manakova, S.Grazulis, D.Matulis. Functionalization of Fluorinated Benzenesulfonamides and Their Inhibitory Properties Toward Carbonic Anhydrases Chemmedchem V. 10 662 2015.
ISSN: ISSN 1860-7179
PubMed: 25758852
DOI: 10.1002/CMDC.201402490