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Sodium in PDB 4d94: Crystal Structure of TEP1R

Protein crystallography data

The structure of Crystal Structure of TEP1R, PDB code: 4d94 was solved by B.V.Le, M.Williams, S.Logarajah, R.H.G.Baxter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.87 / 2.70
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 150.515, 150.515, 226.315, 90.00, 90.00, 90.00
R / Rfree (%) 21.9 / 24.4

Other elements in 4d94:

The structure of Crystal Structure of TEP1R also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of TEP1R (pdb code 4d94). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Crystal Structure of TEP1R, PDB code: 4d94:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 4d94

Go back to Sodium Binding Sites List in 4d94
Sodium binding site 1 out of 2 in the Crystal Structure of TEP1R


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of TEP1R within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na2008

b:47.6
occ:1.00
OE1 A:GLU1061 3.4 59.1 1.0
OE2 A:GLU1061 3.6 58.5 1.0
NZ A:LYS1059 3.6 88.5 1.0
ND2 A:ASN1098 3.9 58.3 1.0
CD A:GLU1061 3.9 57.6 1.0
NE2 A:GLN1099 4.1 45.2 1.0
CD A:LYS1059 4.2 78.5 1.0
CE A:LYS1059 4.5 85.8 1.0
NE1 A:TRP1095 4.5 34.4 1.0
CD1 A:TRP1095 4.5 35.4 1.0

Sodium binding site 2 out of 2 in 4d94

Go back to Sodium Binding Sites List in 4d94
Sodium binding site 2 out of 2 in the Crystal Structure of TEP1R


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Crystal Structure of TEP1R within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na2009

b:78.5
occ:1.00
O A:GLN1323 3.3 88.3 1.0
N A:LEU1296 3.4 48.9 1.0
N A:LYS1297 3.4 47.5 1.0
N A:GLN1323 3.6 0.6 1.0
CA A:LYS1322 3.6 0.9 1.0
CG A:LYS1322 3.6 0.5 1.0
CB A:LYS1322 3.7 0.7 1.0
CD A:LYS1322 3.7 0.3 1.0
CB A:LYS1297 3.8 44.7 1.0
CE A:LYS1322 3.8 0.5 1.0
C A:LYS1322 3.9 0.5 1.0
CA A:LEU1296 3.9 47.7 1.0
C A:ALA1295 4.0 49.1 1.0
CA A:ALA1295 4.0 46.3 1.0
C A:LEU1296 4.0 46.7 1.0
CE A:LYS1297 4.1 51.0 1.0
CG A:LYS1297 4.1 45.9 1.0
CA A:LYS1297 4.1 47.6 1.0
C A:GLN1323 4.2 92.6 1.0
O A:VAL1294 4.3 40.4 1.0
CA A:GLN1323 4.4 93.6 1.0
O A:LYS1297 4.5 51.6 1.0
CD A:LYS1297 4.7 47.1 1.0
CB A:GLN1323 4.7 83.9 1.0
O A:ASP1321 4.8 98.0 1.0
C A:LYS1297 4.8 51.3 1.0
NZ A:LYS1297 4.8 53.8 1.0
CB A:ALA1295 4.9 47.2 1.0
N A:LYS1322 4.9 0.9 1.0
O A:LYS1322 4.9 0.8 1.0
O A:ALA1295 4.9 51.1 1.0

Reference:

B.V.Le, M.Williams, S.Logarajah, R.H.Baxter. Molecular Basis For Genetic Resistance of Anopheles Gambiae to Plasmodium: Structural Analysis of TEP1 Susceptible and Resistant Alleles. Plos Pathog. V. 8 02958 2012.
ISSN: ISSN 1553-7366
PubMed: 23055931
DOI: 10.1371/JOURNAL.PPAT.1002958
Page generated: Mon Oct 7 14:51:29 2024

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