Arsenic in PDB 1z6b: Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A

The structure of Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A, PDB code: 1z6b was solved by D.Kostrewa, F.K.Winkler, G.Folkers, L.Scapozza, R.Perozzo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	87.71 / 2.09
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	90.604, 127.490, 173.673, 90.00, 90.00, 90.00
R / Rfree (%)	17.4 / 22.2

The structure of Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A also contains other interesting chemical elements:

Chlorine

(Cl)

6 atoms

The binding sites of Arsenic atom in the Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A (pdb code 1z6b). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 6 binding sites of Arsenic where determined in the Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A, PDB code: 1z6b:
Jump to Arsenic binding site number: 1; 2; 3; 4; 5; 6;

Arsenic binding site 1 out of 6 in the Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A within 5.0Å range: probe atom residue distance (Å) B Occ A:As402 b:0.3 occ:1.00 AS A:CAC402 0.0 0.3 1.0 O1 A:CAC402 1.7 0.2 1.0 O2 A:CAC402 1.7 0.5 1.0 C1 A:CAC402 2.0 0.9 1.0 C2 A:CAC402 2.0 0.7 1.0 NE2 A:HIS98 3.5 54.4 1.0 OE2 A:GLU147 3.6 65.9 1.0 O A:PHE169 3.7 73.4 1.0 CE2 A:PHE169 4.0 76.5 1.0 OE1 A:GLU147 4.1 66.1 1.0 NE2 B:HIS133 4.1 61.3 1.0 CL B:CL302 4.1 59.0 1.0 CE1 A:HIS98 4.2 60.5 1.0 CZ A:PHE169 4.2 67.4 1.0 CD A:GLU147 4.3 70.8 1.0 CD2 A:PHE169 4.4 86.0 1.0 O A:HOH516 4.5 52.0 1.0 CD2 A:HIS98 4.6 60.7 1.0 N A:PHE171 4.8 66.9 1.0 CE1 A:PHE169 4.8 74.3 1.0 C A:PHE169 4.8 76.0 1.0 CB A:ALA150 4.8 62.2 1.0 CD2 B:HIS133 4.9 71.8 1.0 CZ B:PHE134 4.9 68.1 1.0 CD2 A:PHE171 4.9 56.1 1.0 CG A:GLN151 4.9 64.5 1.0 CG A:PHE169 4.9 83.8 1.0

Arsenic binding site 2 out of 6 in the Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A within 5.0Å range: probe atom residue distance (Å) B Occ B:As401 b:0.5 occ:1.00 AS B:CAC401 0.0 0.5 1.0 O1 B:CAC401 1.7 0.8 1.0 O2 B:CAC401 1.7 0.1 1.0 C2 B:CAC401 2.0 0.5 1.0 C1 B:CAC401 2.0 0.9 1.0 NE2 B:HIS98 3.4 59.2 1.0 OE2 B:GLU147 3.6 67.0 1.0 CL A:CL301 4.1 65.1 1.0 OE1 B:GLU147 4.1 65.0 1.0 CE1 B:HIS98 4.2 61.8 1.0 NE2 A:HIS133 4.2 54.9 1.0 O B:HOH535 4.2 60.9 1.0 CD B:GLU147 4.2 67.8 1.0 O B:HOH515 4.4 47.5 1.0 CD2 B:HIS98 4.4 60.3 1.0 CB B:PHE171 4.6 73.5 1.0 CD2 B:PHE171 4.8 65.8 1.0 CZ A:PHE134 4.8 62.0 1.0 CD2 A:HIS133 4.9 55.5 1.0 CG B:GLN151 4.9 63.4 1.0

Arsenic binding site 3 out of 6 in the Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A within 5.0Å range: probe atom residue distance (Å) B Occ C:As404 b:0.7 occ:1.00 AS C:CAC404 0.0 0.7 1.0 O1 C:CAC404 1.7 0.7 1.0 O2 C:CAC404 1.7 0.8 1.0 C1 C:CAC404 2.0 0.7 1.0 C2 C:CAC404 2.0 0.2 1.0 NE2 C:HIS98 3.6 54.4 1.0 OE2 C:GLU147 3.7 61.5 1.0 CE2 C:PHE169 4.0 90.6 1.0 CE1 C:HIS98 4.2 61.8 1.0 OE1 C:GLU147 4.2 65.9 1.0 CZ C:PHE169 4.2 91.5 1.0 O C:PHE169 4.2 90.5 1.0 CL D:CL304 4.3 57.8 1.0 CD C:GLU147 4.3 67.3 1.0 NE2 D:HIS133 4.4 59.5 1.0 CD2 C:PHE169 4.6 0.1 1.0 O C:HOH510 4.6 45.0 1.0 CD2 C:HIS98 4.7 62.0 1.0 CD2 C:PHE171 4.8 62.7 1.0 N C:PHE171 4.8 69.8 1.0 CB C:ALA150 4.8 60.7 1.0 CE1 C:PHE169 4.8 92.2 1.0 CZ D:PHE134 5.0 62.2 1.0

Arsenic binding site 4 out of 6 in the Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 4 of Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A within 5.0Å range: probe atom residue distance (Å) B Occ D:As403 b:0.6 occ:1.00 AS D:CAC403 0.0 0.6 1.0 O1 D:CAC403 1.7 0.5 1.0 O2 D:CAC403 1.7 0.7 1.0 C1 D:CAC403 2.0 0.8 1.0 C2 D:CAC403 2.0 0.2 1.0 NE2 D:HIS98 3.3 58.5 1.0 OE2 D:GLU147 3.7 68.8 1.0 CE2 D:PHE169 4.0 0.4 1.0 CE1 D:HIS98 4.0 60.2 1.0 O D:PHE169 4.1 94.7 1.0 CL C:CL303 4.1 63.6 1.0 OE1 D:GLU147 4.1 64.2 1.0 NE2 C:HIS133 4.2 56.6 1.0 CD D:GLU147 4.3 73.8 1.0 CD2 D:HIS98 4.4 59.0 1.0 CZ D:PHE169 4.4 0.8 1.0 CD2 D:PHE169 4.5 0.3 1.0 O D:HOH510 4.5 43.3 1.0 CD2 D:PHE171 4.8 59.5 1.0 CZ C:PHE134 4.8 58.9 1.0 CD2 C:HIS133 4.9 57.9 1.0 N D:PHE171 5.0 78.4 1.0

Arsenic binding site 5 out of 6 in the Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 5 of Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A within 5.0Å range: probe atom residue distance (Å) B Occ E:As406 b:0.8 occ:1.00 AS E:CAC406 0.0 0.8 1.0 O1 E:CAC406 1.7 0.9 1.0 O2 E:CAC406 1.7 0.8 1.0 C1 E:CAC406 2.0 0.3 1.0 C2 E:CAC406 2.0 1.0 1.0 NE2 E:HIS98 3.5 57.5 1.0 OE2 E:GLU147 3.6 67.4 1.0 O E:PHE169 3.9 93.2 1.0 CE2 E:PHE169 4.1 0.1 1.0 CE1 E:HIS98 4.2 63.4 1.0 CZ E:PHE169 4.2 99.4 1.0 NE2 F:HIS133 4.2 59.6 1.0 CL F:CL306 4.3 61.2 1.0 OE1 E:GLU147 4.3 77.0 1.0 CD E:GLU147 4.4 69.0 1.0 CD2 E:PHE169 4.6 0.8 1.0 CD2 E:HIS98 4.6 59.8 1.0 O E:HOH524 4.6 51.7 1.0 CB E:ALA150 4.8 61.1 1.0 CD2 E:PHE171 4.8 61.1 1.0 CE1 E:PHE169 4.8 98.7 1.0 N E:PHE171 4.8 75.8 1.0 C E:PHE169 4.9 93.1 1.0 CZ F:PHE134 5.0 60.1 1.0

Arsenic binding site 6 out of 6 in the Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 6 of Crystal Structure of Plasmodium Falciparum Fabz at 2.1 A within 5.0Å range: probe atom residue distance (Å) B Occ F:As405 b:0.3 occ:1.00 AS F:CAC405 0.0 0.3 1.0 O1 F:CAC405 1.7 0.2 1.0 O2 F:CAC405 1.8 0.2 1.0 C1 F:CAC405 2.0 0.5 1.0 C2 F:CAC405 2.0 0.7 1.0 NE2 F:HIS98 3.5 55.4 1.0 OE2 F:GLU147 3.7 64.7 1.0 CE2 F:PHE169 3.8 89.7 1.0 CZ F:PHE169 4.0 86.9 1.0 CE1 F:HIS98 4.2 61.0 1.0 OE1 F:GLU147 4.2 64.4 1.0 NE2 E:HIS133 4.3 56.6 1.0 CL E:CL305 4.3 57.3 1.0 CD F:GLU147 4.4 64.2 1.0 O F:PHE169 4.4 97.3 1.0 CD2 F:PHE169 4.5 93.0 1.0 CD2 F:HIS98 4.6 63.1 1.0 N F:PHE171 4.7 72.2 1.0 O F:HOH511 4.8 43.5 1.0 CE1 F:PHE169 4.8 93.9 1.0 CD2 F:PHE171 4.8 61.1 1.0 CG F:GLN151 4.9 56.5 1.0 CA F:LEU170 4.9 85.0 1.0 CB F:ALA150 4.9 50.6 1.0 CZ E:PHE134 5.0 62.5 1.0

D.Kostrewa, F.K.Winkler, G.Folkers, L.Scapozza, R.Perozzo. The Crystal Structure of Pffabz, the Unique Beta-Hydroxyacyl-Acp Dehydratase Involved in Fatty Acid Biosynthesis of Plasmodium Falciparum Protein Sci. V. 14 1570 2005.
ISSN: ISSN 0961-8368
PubMed: 15930004
DOI: 10.1110/PS.051373005