Atomistry » Sodium » PDB 2isz-2jln » 2izc
Atomistry »
  Sodium »
    PDB 2isz-2jln »
      2izc »

Sodium in PDB 2izc: Apostreptavidin pH 2.0 I222 Complex

Protein crystallography data

The structure of Apostreptavidin pH 2.0 I222 Complex, PDB code: 2izc was solved by B.A.Katz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.50 / 1.40
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 94.850, 105.630, 48.140, 90.00, 90.00, 90.00
R / Rfree (%) 20.7 / 24.1

Other elements in 2izc:

The structure of Apostreptavidin pH 2.0 I222 Complex also contains other interesting chemical elements:

Chlorine (Cl) 3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Apostreptavidin pH 2.0 I222 Complex (pdb code 2izc). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Apostreptavidin pH 2.0 I222 Complex, PDB code: 2izc:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 2izc

Go back to Sodium Binding Sites List in 2izc
Sodium binding site 1 out of 2 in the Apostreptavidin pH 2.0 I222 Complex


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Apostreptavidin pH 2.0 I222 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na504

b:49.1
occ:1.00
O B:HOH507 2.5 39.9 1.0
H2 B:HOH507 3.0 37.4 1.0
H1 B:HOH507 3.2 39.1 1.0
CL B:CL509 3.4 36.6 0.8
HZ2 B:TRP92 3.7 16.4 1.0
CE2 B:TRP108 3.8 14.8 1.0
HG22 B:THR90 3.8 16.9 1.0
CZ2 B:TRP108 3.9 19.8 1.0
NE1 B:TRP108 4.0 17.7 1.0
CD2 B:TRP108 4.1 12.0 1.0
OD2 B:ASP128 4.1 22.4 1.0
HZ2 B:TRP108 4.2 18.7 1.0
HD11 B:LEU110 4.2 16.9 0.4
HE1 B:TRP108 4.2 16.0 1.0
HG23 B:VAL47 4.3 38.8 1.0
HD11 B:LEU25 4.4 32.1 1.0
HE1 B:TRP92 4.4 16.5 1.0
CZ2 B:TRP92 4.4 15.1 1.0
CH2 B:TRP108 4.4 16.4 1.0
CD1 B:TRP108 4.5 17.3 1.0
CG B:TRP108 4.5 14.8 1.0
CE3 B:TRP108 4.6 14.8 1.0
HG21 B:VAL47 4.6 39.0 1.0
HD13 B:LEU25 4.6 31.1 1.0
HG1 B:THR90 4.7 22.5 1.0
HG22 B:VAL47 4.7 38.4 1.0
HD23 B:LEU110 4.7 20.1 0.7
CZ3 B:TRP108 4.7 18.0 1.0
HH B:TYR43 4.7 20.2 1.0
HZ2 B:TRP79 4.8 23.9 1.0
CG2 B:THR90 4.8 16.5 1.0
CG2 B:VAL47 4.8 38.2 1.0
HD12 B:LEU25 4.8 31.4 1.0
OD1 B:ASP128 4.8 29.4 1.0
O B:HOH867 4.8 31.4 1.0
CD1 B:LEU25 4.9 31.3 1.0
CG B:ASP128 4.9 25.0 1.0
HG21 B:THR90 4.9 17.4 1.0
CE2 B:TRP92 4.9 17.7 1.0
NE1 B:TRP92 4.9 16.7 1.0
H2 B:HOH867 5.0 33.6 1.0
HH2 B:TRP108 5.0 16.6 1.0

Sodium binding site 2 out of 2 in 2izc

Go back to Sodium Binding Sites List in 2izc
Sodium binding site 2 out of 2 in the Apostreptavidin pH 2.0 I222 Complex


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Apostreptavidin pH 2.0 I222 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Na508

b:35.8
occ:1.00
CL D:CL505 2.7 72.6 1.1
O D:HOH501 3.0 41.4 1.0
OD2 D:ASP128 3.3 32.5 1.0
HZ2 D:TRP92 3.5 14.7 1.0
H1 D:HOH501 3.6 42.0 1.0
H2 D:HOH501 3.6 42.1 1.0
CE2 D:TRP108 3.7 15.2 1.0
HE1 D:TRP92 3.7 17.1 1.0
NE1 D:TRP108 3.7 15.9 1.0
HE1 D:TRP108 3.9 13.8 1.0
HG22 D:THR90 3.9 15.9 1.0
HD11 D:LEU25 4.0 44.9 1.0
CZ2 D:TRP108 4.1 16.3 1.0
HH D:TYR43 4.1 25.6 1.0
CD2 D:TRP108 4.1 13.7 1.0
CD1 D:TRP108 4.1 16.2 1.0
CZ2 D:TRP92 4.2 16.6 1.0
CG D:ASP128 4.2 29.4 1.0
HZ2 D:TRP108 4.3 13.4 1.0
NE1 D:TRP92 4.3 17.3 1.0
CG D:TRP108 4.3 13.8 1.0
HD13 D:LEU25 4.4 44.6 1.0
HD22 D:ASN23 4.4 37.6 1.0
OD1 D:ASP128 4.5 40.7 1.0
CE2 D:TRP92 4.5 18.7 1.0
HD1 D:TRP108 4.7 13.8 1.0
CD1 D:LEU25 4.7 46.8 1.0
OH D:TYR43 4.7 26.2 1.0
CH2 D:TRP108 4.7 15.1 1.0
CE3 D:TRP108 4.8 13.5 1.0
HG1 D:THR90 4.8 15.7 1.0
CG2 D:THR90 4.9 15.9 1.0
HD21 D:ASN23 4.9 37.7 1.0
HG22 D:VAL47 4.9 53.6 0.8

Reference:

B.A.Katz, B.A.Katz. N/A N/A.
ISSN: ISSN 0022-2836
PubMed: 9405158
DOI: 10.1006/JMBI.1997.1444
Page generated: Mon Oct 7 02:55:14 2024

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy