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Sodium in PDB 2a32: Trypsin in Complex with Benzene Boronic Acid

Enzymatic activity of Trypsin in Complex with Benzene Boronic Acid

All present enzymatic activity of Trypsin in Complex with Benzene Boronic Acid:
3.4.21.4;

Protein crystallography data

The structure of Trypsin in Complex with Benzene Boronic Acid, PDB code: 2a32 was solved by T.R.Transue, S.A.Gabel, R.E.London, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.20 / 1.50
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.849, 53.704, 46.713, 90.00, 90.00, 90.00
R / Rfree (%) 15.8 / 18.8

Other elements in 2a32:

The structure of Trypsin in Complex with Benzene Boronic Acid also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Trypsin in Complex with Benzene Boronic Acid (pdb code 2a32). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Trypsin in Complex with Benzene Boronic Acid, PDB code: 2a32:

Sodium binding site 1 out of 1 in 2a32

Go back to Sodium Binding Sites List in 2a32
Sodium binding site 1 out of 1 in the Trypsin in Complex with Benzene Boronic Acid


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Trypsin in Complex with Benzene Boronic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na810

b:41.4
occ:0.71
H1 A:HOH855 2.0 21.5 0.8
O A:HOH855 2.2 21.5 0.8
O A:HOH1030 2.4 27.9 0.5
O A:HOH1029 2.6 37.4 0.9
O A:HOH918 2.7 27.1 0.9
H1 A:HOH1029 2.8 37.4 0.9
H2 A:HOH1030 2.9 27.9 0.5
H2 A:HOH855 2.9 21.5 0.8
H1 A:HOH1030 3.1 27.9 0.5
H2 A:HOH918 3.1 27.1 0.9
H1 A:HOH1031 3.1 42.4 0.8
H2 A:HOH1029 3.3 37.4 0.9
H1 A:HOH918 3.5 27.1 0.9
HA A:SER171 3.6 11.2 1.0
HB3 A:ASN223 3.8 21.2 1.0
H2 A:HOH1031 3.9 42.4 0.8
O A:SER170 3.9 17.2 1.0
O A:HOH1031 3.9 42.4 0.8
H1 A:HOH1033 4.0 22.2 0.6
O A:HOH1030 4.2 23.9 0.5
H1 A:HOH957 4.4 24.6 0.5
H2 A:HOH1030 4.4 23.9 0.5
H2 A:HOH957 4.4 24.6 0.5
O A:HOH1033 4.5 22.2 0.6
O A:SER171 4.5 15.7 1.0
O A:HOH957 4.6 24.6 0.5
CA A:SER171 4.6 11.2 1.0
HB2 A:ASN223 4.6 21.2 1.0
CB A:ASN223 4.7 21.2 1.0
HE2 A:LYS224 4.7 38.9 1.0
HZ1 A:LYS224 4.8 40.5 1.0
C A:SER170 4.8 17.9 1.0
H1 A:HOH1030 4.9 23.9 0.5
HD3 A:PRO173 4.9 17.2 1.0
C A:SER171 4.9 13.3 1.0
O A:ASN223 4.9 19.4 1.0
HG A:SER170 5.0 22.5 0.3

Reference:

T.R.Transue, S.A.Gabel, R.E.London. uc(Nmr) and Crystallographic Characterization of Adventitious Borate Binding By Trypsin. Bioconjug.Chem. V. 17 300 2006.
ISSN: ISSN 1043-1802
PubMed: 16536459
DOI: 10.1021/BC0502210
Page generated: Mon Oct 7 01:47:45 2024

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