Sodium in PDB 2pn5: Crystal Structure of TEP1R
Protein crystallography data
The structure of Crystal Structure of TEP1R, PDB code: 2pn5
was solved by
R.H.G.Baxter,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Resolution Low / High (Å)
|
45.88 /
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 (%)
|
23.9 /
27.5
|
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of TEP1R
(pdb code 2pn5). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the
Crystal Structure of TEP1R, PDB code: 2pn5:
Jump to Sodium binding site number:
1;
2;
3;
Sodium binding site 1 out
of 3 in 2pn5
Go back to
Sodium Binding Sites List in 2pn5
Sodium binding site 1 out
of 3 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:Na1331
b:21.9
occ:1.00
|
N
|
A:VAL901
|
3.2
|
35.6
|
1.0
|
OG
|
A:SER900
|
3.2
|
33.0
|
1.0
|
OE1
|
A:GLN955
|
3.2
|
33.3
|
1.0
|
N
|
A:PHE902
|
3.3
|
35.0
|
1.0
|
N
|
A:ALA946
|
3.5
|
37.0
|
1.0
|
CA
|
A:LYS945
|
3.7
|
36.5
|
1.0
|
O
|
A:ALA946
|
3.8
|
37.3
|
1.0
|
CB
|
A:PHE902
|
3.8
|
34.3
|
1.0
|
CB
|
A:LYS945
|
3.9
|
36.1
|
1.0
|
C
|
A:SER900
|
3.9
|
35.4
|
1.0
|
CB
|
A:SER900
|
3.9
|
34.1
|
1.0
|
CA
|
A:SER900
|
4.0
|
35.3
|
1.0
|
CA
|
A:VAL901
|
4.0
|
36.1
|
1.0
|
CD
|
A:GLN955
|
4.0
|
33.0
|
1.0
|
CG
|
A:GLN955
|
4.0
|
32.5
|
1.0
|
C
|
A:LYS945
|
4.1
|
37.8
|
1.0
|
C
|
A:VAL901
|
4.2
|
35.3
|
1.0
|
CA
|
A:PHE902
|
4.2
|
34.5
|
1.0
|
CG2
|
A:VAL901
|
4.2
|
35.9
|
1.0
|
CD2
|
A:LEU964
|
4.3
|
32.7
|
1.0
|
CB
|
A:VAL901
|
4.4
|
36.9
|
1.0
|
CG1
|
A:VAL901
|
4.4
|
37.1
|
1.0
|
CA
|
A:ALA946
|
4.5
|
38.0
|
1.0
|
C
|
A:ALA946
|
4.6
|
37.9
|
1.0
|
O
|
A:HOH1417
|
4.6
|
37.7
|
1.0
|
CD1
|
A:LEU964
|
4.7
|
30.6
|
1.0
|
CB
|
A:GLN955
|
4.7
|
34.6
|
1.0
|
N
|
A:LYS945
|
4.9
|
37.5
|
1.0
|
O
|
A:SER900
|
4.9
|
35.4
|
1.0
|
CB
|
A:ALA946
|
4.9
|
37.9
|
1.0
|
OH
|
A:TYR950
|
5.0
|
32.3
|
1.0
|
|
Sodium binding site 2 out
of 3 in 2pn5
Go back to
Sodium Binding Sites List in 2pn5
Sodium binding site 2 out
of 3 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:Na1332
b:44.0
occ:1.00
|
OE1
|
A:GLU1040
|
3.1
|
50.0
|
1.0
|
OE2
|
A:GLU1040
|
3.3
|
49.2
|
1.0
|
CD
|
A:GLU1040
|
3.6
|
48.7
|
1.0
|
ND2
|
A:ASN1077
|
3.7
|
45.5
|
1.0
|
NZ
|
A:LYS1038
|
3.8
|
66.1
|
1.0
|
NE2
|
A:GLN1078
|
3.9
|
41.1
|
1.0
|
CD
|
A:LYS1038
|
4.2
|
62.0
|
1.0
|
CD1
|
A:TRP1074
|
4.4
|
36.5
|
1.0
|
NE1
|
A:TRP1074
|
4.5
|
36.1
|
1.0
|
CE
|
A:LYS1038
|
4.5
|
66.0
|
1.0
|
CG
|
A:ASN1077
|
4.9
|
45.2
|
1.0
|
CD
|
A:GLN1078
|
4.9
|
40.3
|
1.0
|
|
Sodium binding site 3 out
of 3 in 2pn5
Go back to
Sodium Binding Sites List in 2pn5
Sodium binding site 3 out
of 3 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 3 of Crystal Structure of TEP1R within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Na1333
b:53.6
occ:1.00
|
N
|
A:GLN1302
|
3.0
|
75.3
|
1.0
|
N
|
A:LYS1276
|
3.2
|
45.5
|
1.0
|
NZ
|
A:LYS1276
|
3.2
|
44.9
|
1.0
|
N
|
A:LEU1275
|
3.3
|
45.4
|
1.0
|
O
|
A:GLN1302
|
3.3
|
78.2
|
1.0
|
CA
|
A:LYS1301
|
3.3
|
74.1
|
1.0
|
CG
|
A:LYS1276
|
3.4
|
43.2
|
1.0
|
C
|
A:LYS1301
|
3.5
|
74.9
|
1.0
|
CG
|
A:LYS1301
|
3.6
|
76.3
|
1.0
|
CB
|
A:LYS1301
|
3.6
|
75.3
|
1.0
|
C
|
A:ALA1274
|
3.8
|
44.6
|
1.0
|
O
|
A:VAL1273
|
3.8
|
40.5
|
1.0
|
CA
|
A:ALA1274
|
3.8
|
43.5
|
1.0
|
CA
|
A:GLN1302
|
3.9
|
76.2
|
1.0
|
C
|
A:GLN1302
|
4.0
|
77.9
|
1.0
|
CA
|
A:LEU1275
|
4.0
|
46.3
|
1.0
|
CB
|
A:GLN1302
|
4.1
|
75.4
|
1.0
|
C
|
A:LEU1275
|
4.1
|
46.0
|
1.0
|
CB
|
A:LYS1276
|
4.2
|
44.2
|
1.0
|
CA
|
A:LYS1276
|
4.2
|
45.2
|
1.0
|
CE
|
A:LYS1276
|
4.2
|
43.1
|
1.0
|
CD
|
A:LYS1276
|
4.2
|
41.7
|
1.0
|
N
|
A:LYS1301
|
4.6
|
72.1
|
1.0
|
C
|
A:VAL1273
|
4.6
|
41.0
|
1.0
|
O
|
A:LYS1301
|
4.6
|
75.8
|
1.0
|
CD
|
A:LYS1301
|
4.6
|
79.1
|
1.0
|
O
|
A:ASP1300
|
4.6
|
69.4
|
1.0
|
N
|
A:ALA1274
|
4.6
|
42.3
|
1.0
|
O
|
A:ALA1274
|
4.7
|
44.9
|
1.0
|
CB
|
A:ALA1274
|
4.8
|
43.9
|
1.0
|
O
|
A:LYS1276
|
4.9
|
46.5
|
1.0
|
CG
|
A:GLN1302
|
5.0
|
75.0
|
1.0
|
|
Reference:
R.H.G.Baxter,
C.I.Chang,
Y.Chelliah,
S.Blandin,
E.A.Levashina,
J.Deisenhofer.
Structural Basis For Conserved Complement Factor-Like Function in the Antimalarial Protein TEP1 Proc.Natl.Acad.Sci.Usa V. 104 11615 2007.
ISSN: ISSN 0027-8424
PubMed: 17606907
DOI: 10.1073/PNAS.0704967104
Page generated: Mon Oct 7 03:43:42 2024
|