Zinc in PDB 6wvv: Plasmodium Vivax M17 Leucyl Aminopeptidase

All present enzymatic activity of Plasmodium Vivax M17 Leucyl Aminopeptidase:
3.4.11.1;

The structure of Plasmodium Vivax M17 Leucyl Aminopeptidase, PDB code: 6wvv was solved by T.R.Malcolm, N.Drinkwater, S.Mcgowan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.32 / 2.33
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	117.035, 201.549, 166.224, 90.00, 106.01, 90.00
R / Rfree (%)	20.5 / 24.4

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 24;

Binding sites:

The binding sites of Zinc atom in the Plasmodium Vivax M17 Leucyl Aminopeptidase (pdb code 6wvv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 24 binding sites of Zinc where determined in the Plasmodium Vivax M17 Leucyl Aminopeptidase, PDB code: 6wvv:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Zinc binding site 1 out of 24 in the Plasmodium Vivax M17 Leucyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Plasmodium Vivax M17 Leucyl Aminopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn708 b:34.3 occ:0.34 HZ1 A:LYS390 1.7 40.9 1.0 OD2 A:ASP415 2.3 43.7 1.0 NZ A:LYS390 2.5 34.1 1.0 OE2 A:GLU477 2.6 32.2 1.0 HZ2 A:LYS390 2.7 40.9 1.0 ZN A:ZN709 2.7 37.3 0.6 OD2 A:ASP395 2.8 31.6 1.0 HZ3 A:LYS390 3.1 40.9 1.0 CG A:ASP415 3.2 35.7 1.0 HE3 A:LYS390 3.2 37.6 1.0 CE A:LYS390 3.2 31.3 1.0 HE2 A:LYS390 3.3 37.6 1.0 O1 A:SO4710 3.4 32.6 1.0 O A:HOH962 3.5 41.6 1.0 CD A:GLU477 3.5 28.5 1.0 OD1 A:ASP415 3.6 36.7 1.0 CG A:ASP395 3.6 28.6 1.0 HB2 A:ASP395 3.7 28.6 1.0 OE1 A:GLU477 3.7 32.7 1.0 HG13 A:ILE392 3.8 30.8 1.0 H A:GLY478 4.0 29.8 1.0 O3 A:SO4710 4.0 35.6 1.0 CB A:ASP395 4.0 23.8 1.0 HB3 A:ASP395 4.1 28.6 1.0 HB3 A:ASP415 4.1 32.1 1.0 HA3 A:GLY478 4.2 35.4 1.0 CB A:ASP415 4.3 26.8 1.0 O A:THR502 4.3 27.2 1.0 S A:SO4710 4.3 32.1 1.0 O A:HOH979 4.4 36.9 1.0 HG21 A:ILE392 4.4 28.3 1.0 HB A:ILE392 4.5 29.9 1.0 N A:GLY478 4.6 24.8 1.0 OD1 A:ASP395 4.6 25.9 1.0 O A:ASP475 4.6 31.0 1.0 CG1 A:ILE392 4.7 25.6 1.0 CD A:LYS390 4.7 31.4 1.0 HG1 A:THR502 4.7 40.8 1.0 CA A:GLY478 4.8 29.5 1.0 HE3 A:MET412 4.8 36.1 1.0 HB2 A:ASP415 4.8 32.1 1.0 HZ1 A:LYS402 4.8 32.2 1.0 HA2 A:GLY478 4.9 35.4 1.0 CG A:GLU477 4.9 27.6 1.0 HE2 A:MET412 4.9 36.1 1.0 OD1 A:ASP475 4.9 29.2 1.0 HG2 A:GLU477 4.9 33.1 1.0 HG12 A:ILE392 4.9 30.8 1.0 H A:GLU477 4.9 30.9 1.0 HD2 A:LYS390 5.0 37.7 1.0 CB A:ILE392 5.0 24.9 1.0 HD3 A:LYS390 5.0 37.7 1.0

Zinc binding site 2 out of 24 in the Plasmodium Vivax M17 Leucyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Plasmodium Vivax M17 Leucyl Aminopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn709 b:37.3 occ:0.59 OD2 A:ASP395 2.1 31.6 1.0 O A:ASP475 2.2 31.0 1.0 OD1 A:ASP475 2.4 29.2 1.0 OE1 A:GLU477 2.6 32.7 1.0 ZN A:ZN708 2.7 34.3 0.3 O A:HOH962 2.8 41.6 1.0 O1 A:SO4710 3.0 32.6 1.0 CG A:ASP395 3.2 28.6 1.0 OE2 A:GLU477 3.2 32.2 1.0 C A:ASP475 3.3 23.4 1.0 CD A:GLU477 3.3 28.5 1.0 CG A:ASP475 3.4 25.7 1.0 HZ1 A:LYS402 3.5 32.2 1.0 HA A:ASP475 3.5 32.4 1.0 OD1 A:ASP395 3.6 25.9 1.0 H A:GLU477 3.7 30.9 1.0 CA A:ASP475 3.8 27.0 1.0 HE2 A:LYS402 4.0 30.6 1.0 HA A:ALA476 4.1 31.9 1.0 NZ A:LYS402 4.1 26.9 1.0 HZ3 A:LYS402 4.2 32.2 1.0 CB A:ASP475 4.2 23.2 1.0 HZ1 A:LYS390 4.2 40.9 1.0 OD2 A:ASP475 4.2 29.8 1.0 OD2 A:ASP415 4.2 43.7 1.0 H A:GLY478 4.2 29.8 1.0 HA2 A:GLY397 4.3 30.3 1.0 N A:ALA476 4.3 24.6 1.0 S A:SO4710 4.4 32.1 1.0 CE A:LYS402 4.4 25.5 1.0 HD22 A:ASN448 4.4 32.5 1.0 CB A:ASP395 4.4 23.8 1.0 N A:GLU477 4.5 25.7 1.0 HE3 A:LYS402 4.5 30.6 1.0 HB3 A:ASP475 4.5 27.8 1.0 HB2 A:ASP395 4.6 28.6 1.0 HB3 A:ASP395 4.6 28.6 1.0 HZ2 A:LYS390 4.7 40.9 1.0 CA A:ALA476 4.7 26.6 1.0 CG A:GLU477 4.8 27.6 1.0 NZ A:LYS390 4.9 34.1 1.0 O2 A:SO4710 4.9 34.0 1.0 HZ2 A:LYS402 4.9 32.2 1.0 HE2 A:MET412 4.9 36.1 1.0 HB2 A:ASP475 5.0 27.8 1.0 O3 A:SO4710 5.0 35.6 1.0

Zinc binding site 3 out of 24 in the Plasmodium Vivax M17 Leucyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Plasmodium Vivax M17 Leucyl Aminopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn706 b:38.5 occ:0.68 O B:ASP475 2.2 30.5 1.0 OD2 B:ASP395 2.2 33.0 1.0 OE1 B:GLU477 2.4 30.2 1.0 O B:HOH892 2.5 39.6 1.0 OD1 B:ASP475 2.6 26.1 1.0 ZN B:ZN707 2.7 33.2 0.4 O4 B:SO4708 2.8 32.2 1.0 OE2 B:GLU477 3.2 28.9 1.0 CD B:GLU477 3.2 28.8 1.0 C B:ASP475 3.2 27.6 1.0 CG B:ASP395 3.3 26.6 1.0 O B:HOH921 3.4 39.5 1.0 HZ1 B:LYS402 3.4 35.3 1.0 H B:GLU477 3.5 34.3 1.0 HA B:ASP475 3.5 34.7 1.0 CG B:ASP475 3.6 28.0 1.0 OD1 B:ASP395 3.8 27.0 1.0 HZ3 B:LYS402 3.9 35.3 1.0 CA B:ASP475 3.9 28.9 1.0 HZ1 B:LYS390 4.0 36.0 1.0 HA B:ALA476 4.0 32.8 1.0 NZ B:LYS402 4.0 29.4 1.0 H B:GLY478 4.1 30.9 1.0 HE2 B:LYS402 4.1 35.9 1.0 OD2 B:ASP415 4.2 39.5 1.0 S B:SO4708 4.2 34.7 1.0 N B:ALA476 4.3 26.6 1.0 N B:GLU477 4.3 28.6 1.0 CB B:ASP475 4.3 26.2 1.0 HA2 B:GLY397 4.4 29.9 1.0 CE B:LYS402 4.5 29.9 1.0 HD22 B:ASN448 4.5 31.4 1.0 OD2 B:ASP475 4.5 32.1 1.0 HE3 B:LYS402 4.5 35.9 1.0 CB B:ASP395 4.5 26.0 1.0 CA B:ALA476 4.6 27.3 1.0 HB2 B:ASP395 4.6 31.2 1.0 CG B:GLU477 4.6 27.6 1.0 HB3 B:ASP395 4.7 31.2 1.0 HB3 B:ASP475 4.7 31.4 1.0 NZ B:LYS390 4.8 30.0 1.0 O3 B:SO4708 4.8 31.6 1.0 HZ2 B:LYS402 4.8 35.3 1.0 HZ2 B:LYS390 4.8 36.0 1.0 O2 B:SO4708 4.8 32.1 1.0 N B:GLY478 4.9 25.7 1.0 C B:ALA476 4.9 26.8 1.0 HB3 B:GLU477 5.0 32.4 1.0

Zinc binding site 4 out of 24 in the Plasmodium Vivax M17 Leucyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Plasmodium Vivax M17 Leucyl Aminopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn707 b:33.2 occ:0.37 HZ1 B:LYS390 1.8 36.0 1.0 OD2 B:ASP415 2.2 39.5 1.0 OE2 B:GLU477 2.4 28.9 1.0 NZ B:LYS390 2.7 30.0 1.0 ZN B:ZN706 2.7 38.5 0.7 OD2 B:ASP395 2.8 33.0 1.0 CG B:ASP415 3.0 33.5 1.0 HZ2 B:LYS390 3.1 36.0 1.0 HZ3 B:LYS390 3.1 36.0 1.0 HE3 B:LYS390 3.2 33.4 1.0 HE2 B:LYS390 3.3 33.4 1.0 CE B:LYS390 3.3 27.8 1.0 O4 B:SO4708 3.4 32.2 1.0 CD B:GLU477 3.4 28.8 1.0 O B:HOH892 3.5 39.6 1.0 HB2 B:ASP395 3.5 31.2 1.0 CG B:ASP395 3.5 26.6 1.0 OD1 B:ASP415 3.6 36.0 1.0 O B:HOH921 3.6 39.5 1.0 OE1 B:GLU477 3.7 30.2 1.0 HG13 B:ILE392 3.7 31.1 1.0 HB3 B:ASP415 3.8 34.1 1.0 CB B:ASP395 3.9 26.0 1.0 HB3 B:ASP395 3.9 31.2 1.0 CB B:ASP415 4.1 28.4 1.0 H B:GLY478 4.1 30.9 1.0 O2 B:SO4708 4.1 32.1 1.0 O B:HOH950 4.3 43.2 1.0 HG21 B:ILE392 4.3 34.3 1.0 HA3 B:GLY478 4.3 30.4 1.0 HB B:ILE392 4.3 34.8 1.0 S B:SO4708 4.4 34.7 1.0 O B:THR502 4.5 32.6 1.0 OD1 B:ASP395 4.5 27.0 1.0 HB2 B:ASP415 4.5 34.1 1.0 HZ1 B:LYS402 4.5 35.3 1.0 CG1 B:ILE392 4.6 25.9 1.0 N B:GLY478 4.6 25.7 1.0 O B:ASP475 4.7 30.5 1.0 CD B:LYS390 4.8 28.2 1.0 HG1 B:THR502 4.8 37.4 1.0 CG B:GLU477 4.8 27.6 1.0 HG2 B:GLU477 4.8 33.1 1.0 HG12 B:ILE392 4.8 31.1 1.0 CB B:ILE392 4.8 29.0 1.0 CA B:GLY478 4.9 25.3 1.0 HA2 B:GLY478 4.9 30.4 1.0 H B:GLU477 4.9 34.3 1.0

Zinc binding site 5 out of 24 in the Plasmodium Vivax M17 Leucyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Plasmodium Vivax M17 Leucyl Aminopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn704 b:28.7 occ:0.29 HZ1 C:LYS390 1.7 35.9 1.0 OD2 C:ASP415 2.0 49.5 1.0 OE2 C:GLU477 2.4 29.9 1.0 NZ C:LYS390 2.5 29.9 1.0 OD2 C:ASP395 2.7 33.4 1.0 HZ2 C:LYS390 2.8 35.9 1.0 ZN C:ZN705 2.9 47.2 0.8 HE3 C:LYS390 2.9 33.9 1.0 CG C:ASP415 3.1 35.2 1.0 HZ3 C:LYS390 3.1 35.9 1.0 CE C:LYS390 3.1 28.2 1.0 HE2 C:LYS390 3.2 33.9 1.0 CD C:GLU477 3.3 28.9 1.0 O4 C:SO4706 3.3 28.9 1.0 HB2 C:ASP395 3.5 33.7 1.0 CG C:ASP395 3.5 28.2 1.0 OE1 C:GLU477 3.6 30.9 1.0 O C:HOH970 3.6 43.3 1.0 HG13 C:ILE392 3.6 35.4 1.0 OD1 C:ASP415 3.7 41.2 1.0 HB3 C:ASP415 3.8 35.5 1.0 H C:GLY478 3.9 34.4 1.0 CB C:ASP395 3.9 28.1 1.0 HB3 C:ASP395 4.0 33.7 1.0 CB C:ASP415 4.1 29.6 1.0 O2 C:SO4706 4.1 33.4 1.0 HA3 C:GLY478 4.1 35.0 1.0 HG21 C:ILE392 4.2 35.3 1.0 HB C:ILE392 4.2 28.5 1.0 HO4 C:PEG702 4.2 62.2 1.0 S C:SO4706 4.3 38.2 1.0 CG1 C:ILE392 4.4 29.5 1.0 N C:GLY478 4.5 28.6 1.0 OD1 C:ASP395 4.5 27.3 1.0 O C:THR502 4.5 33.1 1.0 O4 C:PEG702 4.5 51.9 1.0 HB2 C:ASP415 4.6 35.5 1.0 CD C:LYS390 4.6 30.6 1.0 HG12 C:ILE392 4.6 35.4 1.0 CA C:GLY478 4.7 29.2 1.0 CG C:GLU477 4.7 23.9 1.0 HZ1 C:LYS402 4.7 41.8 1.0 HG2 C:GLU477 4.7 28.8 1.0 CB C:ILE392 4.7 23.7 1.0 HA2 C:GLY478 4.7 35.0 1.0 HG1 C:THR502 4.7 46.6 1.0 HD2 C:LYS390 4.8 36.7 1.0 H C:GLU477 4.8 31.5 1.0 O C:ASP475 4.8 30.1 1.0 CG2 C:ILE392 4.9 29.4 1.0 HD3 C:LYS390 5.0 36.7 1.0

Zinc binding site 6 out of 24 in the Plasmodium Vivax M17 Leucyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Plasmodium Vivax M17 Leucyl Aminopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn705 b:47.2 occ:0.83 OD2 C:ASP395 2.2 33.4 1.0 O C:ASP475 2.2 30.1 1.0 OE1 C:GLU477 2.4 30.9 1.0 OD1 C:ASP475 2.5 27.4 1.0 ZN C:ZN704 2.9 28.7 0.3 O4 C:SO4706 3.0 28.9 1.0 CG C:ASP395 3.2 28.2 1.0 C C:ASP475 3.2 23.6 1.0 CD C:GLU477 3.3 28.9 1.0 HZ1 C:LYS402 3.3 41.8 1.0 O4 C:PEG702 3.3 51.9 1.0 OE2 C:GLU477 3.3 29.9 1.0 HA C:ASP475 3.4 27.8 1.0 CG C:ASP475 3.5 27.7 1.0 H C:GLU477 3.6 31.5 1.0 O C:HOH970 3.6 43.3 1.0 HO4 C:PEG702 3.6 62.2 1.0 OD1 C:ASP395 3.6 27.3 1.0 CA C:ASP475 3.8 23.1 1.0 HZ3 C:LYS402 3.9 41.8 1.0 NZ C:LYS402 3.9 34.8 1.0 HE2 C:LYS402 4.0 33.7 1.0 HZ1 C:LYS390 4.0 35.9 1.0 HA C:ALA476 4.1 30.2 1.0 OD2 C:ASP415 4.1 49.5 1.0 H C:GLY478 4.2 34.4 1.0 CB C:ASP475 4.2 26.5 1.0 N C:ALA476 4.3 26.4 1.0 S C:SO4706 4.3 38.2 1.0 HA2 C:GLY397 4.4 29.7 1.0 HD22 C:ASN448 4.4 30.3 1.0 OD2 C:ASP475 4.4 27.4 1.0 N C:GLU477 4.4 26.2 1.0 CE C:LYS402 4.4 28.1 1.0 HE3 C:LYS402 4.4 33.7 1.0 H41 C:PEG702 4.4 57.6 1.0 CB C:ASP395 4.5 28.1 1.0 C4 C:PEG702 4.5 48.0 1.0 HB2 C:ASP395 4.6 33.7 1.0 HB3 C:ASP475 4.6 31.8 1.0 CA C:ALA476 4.6 25.1 1.0 O1 C:SO4706 4.6 38.1 1.0 HB3 C:ASP395 4.7 33.7 1.0 HZ2 C:LYS402 4.7 41.8 1.0 HZ2 C:LYS390 4.7 35.9 1.0 CG C:GLU477 4.7 23.9 1.0 NZ C:LYS390 4.8 29.9 1.0 HB3 C:GLU477 5.0 37.4 1.0 N C:GLY478 5.0 28.6 1.0 O2 C:SO4706 5.0 33.4 1.0

Zinc binding site 7 out of 24 in the Plasmodium Vivax M17 Leucyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 7 of Plasmodium Vivax M17 Leucyl Aminopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn705 b:44.8 occ:0.81 OD2 D:ASP395 2.1 26.8 1.0 O D:ASP475 2.2 28.8 1.0 OE1 D:GLU477 2.4 29.1 1.0 O D:HOH915 2.5 37.8 1.0 OD1 D:ASP475 2.6 26.1 1.0 ZN D:ZN706 2.7 30.1 0.3 O1 D:SO4707 2.9 34.9 1.0 O D:HOH929 3.1 40.1 1.0 CD D:GLU477 3.2 25.9 1.0 CG D:ASP395 3.2 27.8 1.0 OE2 D:GLU477 3.2 32.4 1.0 C D:ASP475 3.3 29.0 1.0 HZ1 D:LYS402 3.4 39.5 1.0 H D:GLU477 3.5 34.3 1.0 HA D:ASP475 3.6 31.9 1.0 CG D:ASP475 3.6 28.9 1.0 OD1 D:ASP395 3.6 26.9 1.0 HZ1 D:LYS390 3.8 40.1 1.0 CA D:ASP475 3.9 26.6 1.0 HA D:ALA476 4.0 33.3 1.0 HE2 D:LYS402 4.1 31.3 1.0 OD2 D:ASP415 4.1 41.6 1.0 NZ D:LYS402 4.1 32.9 1.0 H D:GLY478 4.2 40.5 1.0 HZ3 D:LYS402 4.2 39.5 1.0 S D:SO4707 4.2 37.1 1.0 N D:GLU477 4.3 28.5 1.0 CB D:ASP475 4.3 28.3 1.0 N D:ALA476 4.3 30.3 1.0 HA2 D:GLY397 4.4 29.8 1.0 OD2 D:ASP475 4.4 29.8 1.0 HD22 D:ASN448 4.4 34.5 1.0 CB D:ASP395 4.5 25.8 1.0 CE D:LYS402 4.5 26.1 1.0 HE3 D:LYS402 4.5 31.3 1.0 NZ D:LYS390 4.6 33.4 1.0 CA D:ALA476 4.6 27.7 1.0 HB2 D:ASP395 4.6 31.0 1.0 CG D:GLU477 4.6 24.5 1.0 O3 D:SO4707 4.6 31.3 1.0 HB3 D:ASP395 4.6 31.0 1.0 HZ2 D:LYS390 4.7 40.1 1.0 HB3 D:ASP475 4.7 34.0 1.0 HB3 D:GLU477 4.9 31.2 1.0 HZ2 D:LYS402 4.9 39.5 1.0 HZ3 D:LYS390 4.9 40.1 1.0 O4 D:SO4707 5.0 37.9 1.0 N D:GLY478 5.0 33.7 1.0 C D:ALA476 5.0 27.1 1.0

Zinc binding site 8 out of 24 in the Plasmodium Vivax M17 Leucyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 8 of Plasmodium Vivax M17 Leucyl Aminopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn706 b:30.1 occ:0.35 HZ1 D:LYS390 1.6 40.1 1.0 OD2 D:ASP415 1.9 41.6 1.0 OE2 D:GLU477 2.2 32.4 1.0 NZ D:LYS390 2.5 33.4 1.0 OD2 D:ASP395 2.6 26.8 1.0 ZN D:ZN705 2.7 44.8 0.8 HZ3 D:LYS390 2.9 40.1 1.0 HZ2 D:LYS390 3.0 40.1 1.0 CG D:ASP415 3.0 34.6 1.0 HE3 D:LYS390 3.1 34.6 1.0 O D:HOH929 3.1 40.1 1.0 CD D:GLU477 3.2 25.9 1.0 CE D:LYS390 3.2 28.9 1.0 HE2 D:LYS390 3.3 34.6 1.0 O1 D:SO4707 3.3 34.9 1.0 CG D:ASP395 3.3 27.8 1.0 HB2 D:ASP395 3.4 31.0 1.0 OE1 D:GLU477 3.5 29.1 1.0 HG13 D:ILE392 3.5 30.2 1.0 O D:HOH915 3.6 37.8 1.0 OD1 D:ASP415 3.7 31.7 1.0 CB D:ASP395 3.8 25.8 1.0 HB3 D:ASP415 3.9 34.9 1.0 HB3 D:ASP395 3.9 31.0 1.0 H D:GLY478 3.9 40.5 1.0 CB D:ASP415 4.1 29.0 1.0 HG21 D:ILE392 4.2 32.1 1.0 HB D:ILE392 4.2 33.2 1.0 O4 D:SO4707 4.3 37.9 1.0 OD1 D:ASP395 4.3 26.9 1.0 HA3 D:GLY478 4.4 33.7 1.0 O D:HOH939 4.4 42.0 1.0 CG1 D:ILE392 4.4 25.2 1.0 O D:THR502 4.4 31.8 1.0 S D:SO4707 4.4 37.1 1.0 HG1 D:THR502 4.5 33.8 1.0 HB2 D:ASP415 4.5 34.9 1.0 N D:GLY478 4.5 33.7 1.0 CG D:GLU477 4.5 24.5 1.0 HG2 D:GLU477 4.6 29.4 1.0 CD D:LYS390 4.7 30.1 1.0 HG12 D:ILE392 4.7 30.2 1.0 CB D:ILE392 4.7 27.6 1.0 H D:GLU477 4.7 34.3 1.0 O D:ASP475 4.8 28.8 1.0 HZ1 D:LYS402 4.8 39.5 1.0 CA D:GLY478 4.9 28.1 1.0 HD2 D:LYS390 4.9 36.1 1.0 CG2 D:ILE392 4.9 26.7 1.0 HA2 D:GLY478 4.9 33.7 1.0 HG3 D:GLU477 5.0 29.4 1.0 OD1 D:ASP475 5.0 26.1 1.0

Zinc binding site 9 out of 24 in the Plasmodium Vivax M17 Leucyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 9 of Plasmodium Vivax M17 Leucyl Aminopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn709 b:32.1 occ:0.35 HZ1 E:LYS390 1.7 36.3 1.0 OD2 E:ASP415 2.0 46.7 1.0 OE2 E:GLU477 2.5 23.9 1.0 NZ E:LYS390 2.5 30.3 1.0 OD2 E:ASP395 2.7 28.2 1.0 ZN E:ZN710 2.7 43.2 0.8 HZ2 E:LYS390 2.8 36.3 1.0 O E:HOH937 3.0 45.0 1.0 HZ3 E:LYS390 3.1 36.3 1.0 HE3 E:LYS390 3.1 33.8 1.0 CG E:ASP415 3.2 39.0 1.0 CE E:LYS390 3.2 28.1 1.0 O2 E:SO4711 3.2 33.5 1.0 HE2 E:LYS390 3.3 33.8 1.0 CD E:GLU477 3.3 28.0 1.0 O E:HOH871 3.4 34.1 1.0 OE1 E:GLU477 3.5 28.8 1.0 CG E:ASP395 3.5 25.1 1.0 HB2 E:ASP395 3.6 29.6 1.0 HG13 E:ILE392 3.8 32.4 1.0 OD1 E:ASP415 3.8 42.5 1.0 H E:GLY478 3.8 34.2 1.0 HB3 E:ASP415 4.0 34.5 1.0 CB E:ASP395 4.0 24.6 1.0 HB3 E:ASP395 4.2 29.6 1.0 O3 E:SO4711 4.2 39.1 1.0 CB E:ASP415 4.2 28.7 1.0 HA3 E:GLY478 4.3 35.2 1.0 S E:SO4711 4.3 38.7 1.0 HG21 E:ILE392 4.3 29.1 1.0 OD1 E:ASP395 4.4 24.4 1.0 HB E:ILE392 4.4 28.0 1.0 O E:THR502 4.4 35.9 1.0 N E:GLY478 4.5 28.5 1.0 O E:HOH934 4.6 45.1 1.0 CG1 E:ILE392 4.6 27.0 1.0 CG E:GLU477 4.6 24.6 1.0 CD E:LYS390 4.6 29.2 1.0 O E:ASP475 4.7 31.3 1.0 HG2 E:GLU477 4.7 29.5 1.0 HG1 E:THR502 4.7 41.2 1.0 H E:GLU477 4.7 32.0 1.0 HB2 E:ASP415 4.7 34.5 1.0 CA E:GLY478 4.8 29.3 1.0 HZ1 E:LYS402 4.8 37.2 1.0 HA2 E:GLY478 4.8 35.2 1.0 HG12 E:ILE392 4.9 32.4 1.0 CB E:ILE392 4.9 23.3 1.0 HD2 E:LYS390 4.9 35.1 1.0 OD1 E:ASP475 5.0 29.2 1.0 HD3 E:LYS390 5.0 35.1 1.0

Zinc binding site 10 out of 24 in the Plasmodium Vivax M17 Leucyl Aminopeptidase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 10 of Plasmodium Vivax M17 Leucyl Aminopeptidase within 5.0Å range: probe atom residue distance (Å) B Occ E:Zn710 b:43.2 occ:0.80 OD2 E:ASP395 2.2 28.2 1.0 O E:ASP475 2.2 31.3 1.0 OD1 E:ASP475 2.4 29.2 1.0 OE1 E:GLU477 2.5 28.8 1.0 O E:HOH871 2.7 34.1 1.0 ZN E:ZN709 2.7 32.1 0.3 O2 E:SO4711 3.0 33.5 1.0 O E:HOH937 3.1 45.0 1.0 CG E:ASP395 3.2 25.1 1.0 CD E:GLU477 3.2 28.0 1.0 OE2 E:GLU477 3.2 23.9 1.0 C E:ASP475 3.3 25.8 1.0 CG E:ASP475 3.5 28.4 1.0 H E:GLU477 3.5 32.0 1.0 HZ1 E:LYS402 3.5 37.2 1.0 OD1 E:ASP395 3.5 24.4 1.0 HA E:ASP475 3.6 29.8 1.0 CA E:ASP475 3.9 24.8 1.0 HA E:ALA476 4.0 34.0 1.0 HE2 E:LYS402 4.0 40.6 1.0 HZ3 E:LYS402 4.0 37.2 1.0 HZ1 E:LYS390 4.1 36.3 1.0 NZ E:LYS402 4.1 31.0 1.0 OD2 E:ASP415 4.2 46.7 1.0 H E:GLY478 4.2 34.2 1.0 CB E:ASP475 4.2 24.4 1.0 OD2 E:ASP475 4.3 33.9 1.0 N E:GLU477 4.3 26.7 1.0 N E:ALA476 4.3 28.1 1.0 S E:SO4711 4.4 38.7 1.0 HD22 E:ASN448 4.4 29.3 1.0 HA2 E:GLY397 4.4 32.7 1.0 CE E:LYS402 4.5 33.9 1.0 HE3 E:LYS402 4.5 40.6 1.0 CB E:ASP395 4.5 24.6 1.0 CA E:ALA476 4.6 28.3 1.0 HB3 E:ASP475 4.6 29.4 1.0 HB2 E:ASP395 4.7 29.6 1.0 CG E:GLU477 4.7 24.6 1.0 HZ2 E:LYS390 4.7 36.3 1.0 HB3 E:ASP395 4.7 29.6 1.0 O4 E:SO4711 4.8 38.0 1.0 NZ E:LYS390 4.8 30.3 1.0 HZ2 E:LYS402 4.9 37.2 1.0 HB3 E:GLU477 4.9 30.0 1.0 C E:ALA476 5.0 27.9 1.0

T.R.Malcolm, M.J.Belousoff, H.Venugopal, N.A.Borg, N.Drinkwater, S.C.Atkinson, S.Mcgowan. Active Site Metals Mediate An Oligomeric Equilibrium in /Plasmodium/ M17 Aminopeptidases J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X