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Chlorine in PDB 1z40: AMA1 From Plasmodium Falciparum

Protein crystallography data

The structure of AMA1 From Plasmodium Falciparum, PDB code: 1z40 was solved by T.Bai, M.Becker, A.Gupta, P.Strike, V.J.Murphy, R.F.Anders, A.H.Batchelor, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.22 / 1.90
Space group P 31
Cell size a, b, c (Å), α, β, γ (°) 54.124, 54.124, 214.144, 90.00, 90.00, 120.00
R / Rfree (%) 19.2 / 23.6

Chlorine Binding Sites:

The binding sites of Chlorine atom in the AMA1 From Plasmodium Falciparum (pdb code 1z40). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the AMA1 From Plasmodium Falciparum, PDB code: 1z40:

Chlorine binding site 1 out of 1 in 1z40

Go back to Chlorine Binding Sites List in 1z40
Chlorine binding site 1 out of 1 in the AMA1 From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of AMA1 From Plasmodium Falciparum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl1

b:53.5
occ:1.00
NZ A:LYS391 2.9 40.6 1.0
N A:TYR390 3.2 42.9 1.0
N A:ARG389 3.6 48.6 1.0
CG A:LYS391 3.7 36.9 1.0
C A:ASP388 3.7 50.2 1.0
N A:ASP388 3.8 51.3 1.0
CD1 A:TYR390 3.9 43.2 1.0
CB A:TYR390 3.9 42.2 1.0
CA A:TYR390 3.9 42.0 1.0
CA A:ASP388 3.9 50.8 1.0
N A:LYS391 4.1 38.5 1.0
CE A:LYS391 4.1 41.2 1.0
C A:TYR390 4.1 40.5 1.0
O A:HOH495 4.2 33.5 1.0
NH2 A:ARG143 4.2 33.3 1.0
CG A:TYR390 4.2 43.8 1.0
CD A:LYS391 4.2 39.4 1.0
C A:ARG389 4.3 45.8 1.0
O A:ASP388 4.3 51.0 1.0
CA A:ARG389 4.4 46.9 1.0
CG A:ARG389 4.5 48.8 1.0
CZ A:ARG143 4.6 34.0 1.0
NE A:ARG143 4.7 33.6 1.0
CB A:LYS391 4.7 37.4 1.0
CE1 A:TYR390 4.8 45.2 1.0
O A:TYR390 4.9 42.0 1.0
CA A:LYS391 4.9 36.0 1.0

Reference:

T.Bai, M.Becker, A.Gupta, P.Strike, V.J.Murphy, R.F.Anders, A.H.Batchelor. Structure of AMA1 From Plasmodium Falciparum Reveals A Clustering of Polymorphisms That Surround A Conserved Hydrophobic Pocket Proc.Natl.Acad.Sci.Usa V. 102 12736 2005.
ISSN: ISSN 0027-8424
PubMed: 16129835
DOI: 10.1073/PNAS.0501808102
Page generated: Sat Jul 20 04:33:39 2024

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