Zinc in PDB 3fns: Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum

The structure of Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum, PDB code: 3fns was solved by P.Bhaumik, A.Gustchina, A.Wlodawer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.50
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	89.800, 89.800, 198.700, 90.00, 90.00, 90.00
R / Rfree (%)	22.5 / 27.4

The binding sites of Zinc atom in the Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum (pdb code 3fns). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum, PDB code: 3fns:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in the Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn329 b:36.6 occ:1.00 O A:HOH374 2.0 32.3 1.0 OE2 B:GLU278A 2.1 49.1 1.0 NE2 A:HIS32 2.1 33.2 1.0 OD2 A:ASP215 2.1 31.6 1.0 OD1 A:ASP215 2.8 36.6 1.0 CD B:GLU278A 2.8 50.4 1.0 CG A:ASP215 2.8 33.9 1.0 OE1 B:GLU278A 2.8 51.6 1.0 CE1 A:HIS32 2.9 32.2 1.0 CD2 A:HIS32 3.2 32.4 1.0 ND1 A:HIS32 4.0 33.9 1.0 CB A:ALA217 4.0 36.8 1.0 CG A:HIS32 4.2 33.8 1.0 CG B:GLU278A 4.2 50.3 1.0 CB A:ALA34 4.2 35.5 1.0 CB A:ASP215 4.3 32.9 1.0 O A:HOH387 4.5 40.1 1.0 OG1 A:THR218 4.7 39.3 1.0 CA A:ALA217 5.0 36.8 1.0

Zinc binding site 2 out of 6 in the Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn330 b:49.9 occ:0.70 OD2 A:ASP195 1.9 39.8 1.0 NE2 A:HIS198 2.1 27.9 1.0 CG A:ASP195 2.7 37.3 1.0 CE1 A:HIS198 2.8 26.4 1.0 OD1 A:ASP195 2.9 37.7 1.0 CD2 A:HIS198 3.3 30.3 1.0 ND1 A:HIS198 4.0 28.9 1.0 CB A:ASP195 4.2 33.6 1.0 CG A:HIS198 4.3 30.2 1.0 NH2 A:ARG261 4.4 33.4 1.0 CB A:SER206 4.5 38.5 1.0 NE A:ARG261 4.5 34.0 1.0 CG A:LYS208 4.5 48.2 1.0 OG A:SER206 4.6 39.5 1.0 CZ A:ARG261 4.6 35.3 1.0 NZ A:LYS208 4.9 52.8 1.0

Zinc binding site 3 out of 6 in the Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn331 b:71.2 occ:0.40 OD1 A:ASP187 2.5 62.9 1.0 OD2 A:ASP127 2.6 59.6 1.0 CG A:ASP187 3.6 61.1 1.0 NE2 A:HIS186 3.6 61.8 1.0 CG A:ASP127 3.7 56.2 1.0 CD2 A:HIS186 3.7 61.0 1.0 OD2 A:ASP187 4.0 61.9 1.0 CB A:ASP127 4.2 53.6 1.0 CE1 A:HIS186 4.4 60.8 1.0 CD2 A:LEU188 4.5 57.2 1.0 CG A:HIS186 4.6 60.9 1.0 N A:ASP187 4.6 57.8 1.0 C A:ASP187 4.6 56.6 1.0 O A:ASP187 4.7 56.6 1.0 OD1 A:ASP127 4.8 57.7 1.0 CB A:ASP187 4.8 58.1 1.0 CA A:ASP187 4.9 57.7 1.0 CD1 A:LEU188 4.9 57.3 1.0 O A:HOH345 4.9 38.2 1.0 ND1 A:HIS186 4.9 61.8 1.0 N A:LEU188 5.0 55.8 1.0

Zinc binding site 4 out of 6 in the Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn332 b:71.7 occ:0.40 OE1 A:GLU51 1.8 74.8 1.0 OE1 A:GLU48 2.0 71.3 1.0 OE2 A:GLU48 2.3 71.2 1.0 CD A:GLU48 2.4 71.2 1.0 CD A:GLU51 2.7 73.9 1.0 OE2 A:GLU51 3.1 73.7 1.0 CG A:GLU48 3.9 70.8 1.0 CG A:GLU51 4.1 71.3 1.0 CB A:GLU48 4.4 69.9 1.0 CA A:GLU48 4.5 69.5 1.0 O A:GLU48 4.8 69.5 1.0

Zinc binding site 5 out of 6 in the Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn329 b:49.0 occ:1.00 O A:HOH336 1.7 21.6 1.0 NE2 B:HIS32 2.0 35.6 1.0 OD2 B:ASP215 2.0 39.0 1.0 OE2 A:GLU278A 2.0 53.6 1.0 CG B:ASP215 2.6 37.5 1.0 OD1 B:ASP215 2.7 36.2 1.0 CE1 B:HIS32 2.9 36.5 1.0 CD A:GLU278A 2.9 52.7 1.0 CD2 B:HIS32 3.0 36.7 1.0 OE1 A:GLU278A 3.1 52.0 1.0 ND1 B:HIS32 4.0 36.3 1.0 CB B:ALA34 4.0 39.8 1.0 CB B:ALA217 4.1 39.0 1.0 CB B:ASP215 4.1 36.7 1.0 CG B:HIS32 4.1 36.7 1.0 CG A:GLU278A 4.3 51.6 1.0 OG1 B:THR218 4.7 41.0 1.0 CA B:ALA217 5.0 39.0 1.0 N B:ALA217 5.0 38.8 1.0

Zinc binding site 6 out of 6 in the Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Crystal Structure of Histo-Aspartic Protease (Hap) From Plasmodium Falciparum within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn330 b:65.1 occ:0.70 OD2 B:ASP195 2.0 41.5 1.0 NE2 B:HIS198 2.1 30.5 1.0 CE1 B:HIS198 2.7 28.1 1.0 CG B:ASP195 2.9 38.8 1.0 OD1 B:ASP195 3.0 44.1 1.0 CD2 B:HIS198 3.3 30.4 1.0 ND1 B:HIS198 4.0 30.7 1.0 CG B:HIS198 4.2 30.9 1.0 CB B:ASP195 4.3 34.7 1.0 NH2 B:ARG261 4.4 34.1 1.0 CG B:LYS208 4.5 47.8 1.0 NE B:ARG261 4.6 34.0 1.0 OG B:SER206 4.6 40.1 1.0 O B:HOH356 4.6 38.1 1.0 CB B:SER206 4.7 39.4 1.0 CZ B:ARG261 4.7 35.2 1.0 CD B:LYS208 4.9 53.5 1.0

P.Bhaumik, H.Xiao, C.L.Parr, Y.Kiso, A.Gustchina, R.Y.Yada, A.Wlodawer. Crystal Structures of the Histo-Aspartic Protease (Hap) From Plasmodium Falciparum. J.Mol.Biol. V. 388 520 2009.
ISSN: ISSN 0022-2836
PubMed: 19285084
DOI: 10.1016/J.JMB.2009.03.011