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Sodium in PDB 2aer: Crystal Structure of Benzamidine-Factor Viia/Soluble Tissue Factor Complex.

Enzymatic activity of Crystal Structure of Benzamidine-Factor Viia/Soluble Tissue Factor Complex.

All present enzymatic activity of Crystal Structure of Benzamidine-Factor Viia/Soluble Tissue Factor Complex.:
3.4.21.21;

Protein crystallography data

The structure of Crystal Structure of Benzamidine-Factor Viia/Soluble Tissue Factor Complex., PDB code: 2aer was solved by S.P.Bajaj, A.E.Schmidt, K.Padmanabhan, M.S.Bajaj, A.Liesum, J.Dumas, D.Prevost, H.Schreuder, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.00 / 1.87
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 69.900, 81.200, 125.900, 90.00, 90.00, 90.00
R / Rfree (%) 19.1 / 25.6

Other elements in 2aer:

The structure of Crystal Structure of Benzamidine-Factor Viia/Soluble Tissue Factor Complex. also contains other interesting chemical elements:

Magnesium (Mg) 3 atoms
Zinc (Zn) 2 atoms
Calcium (Ca) 6 atoms
Chlorine (Cl) 3 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Benzamidine-Factor Viia/Soluble Tissue Factor Complex. (pdb code 2aer). 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 Crystal Structure of Benzamidine-Factor Viia/Soluble Tissue Factor Complex., PDB code: 2aer:

Sodium binding site 1 out of 1 in 2aer

Go back to Sodium Binding Sites List in 2aer
Sodium binding site 1 out of 1 in the Crystal Structure of Benzamidine-Factor Viia/Soluble Tissue Factor Complex.


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 Benzamidine-Factor Viia/Soluble Tissue Factor Complex. within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Na3010

b:22.5
occ:1.00
O H:TYR184 2.5 13.3 1.0
O H:HOH3113 2.5 43.7 1.0
N H:GLY187 2.7 16.1 1.0
O H:THR221 2.7 15.1 1.0
C H:SER185 3.1 15.4 1.0
O H:HOH3068 3.1 20.9 1.0
CA H:SER185 3.2 14.7 1.0
O H:HIS224 3.2 14.2 1.0
CA H:GLY187 3.3 15.6 1.0
O H:SER185 3.3 15.0 1.0
N H:ASP186 3.3 16.2 1.0
C H:TYR184 3.4 13.4 1.0
C H:THR221 3.4 15.3 1.0
C H:ALA221A 3.6 14.2 1.0
N H:SER185 3.7 14.1 1.0
N H:THR221 3.7 15.2 1.0
C H:ASP186 3.8 16.8 1.0
CA H:ALA221A 3.9 14.2 1.0
O H:ALA221A 4.0 15.0 1.0
N H:VAL222 4.0 14.5 1.0
CA H:ASP186 4.1 16.8 1.0
CA H:VAL222 4.1 14.2 1.0
CA H:THR221 4.2 15.8 1.0
C H:GLY187 4.3 15.9 1.0
C H:HIS224 4.3 12.8 1.0
N H:SER188A 4.4 14.5 1.0
CB H:SER185 4.5 14.2 1.0
OD1 H:ASP186 4.6 17.4 1.0
N H:HIS224 4.6 13.2 1.0
N H:GLY223 4.7 13.8 1.0
CA H:TYR184 4.7 12.4 1.0
C H:VAL222 4.8 13.8 1.0
CB H:ALA221A 4.8 13.4 1.0
O H:HOH3062 4.8 8.2 1.0
O H:HOH3192 4.8 16.2 1.0
CB H:TYR184 4.9 12.9 1.0
O H:ASP186 5.0 17.6 1.0
O H:LYS188 5.0 13.8 1.0
CA H:HIS224 5.0 12.8 1.0

Reference:

S.P.Bajaj, A.E.Schmidt, S.Agah, M.S.Bajaj, K.Padmanabhan. High Resolution Structures of P-Aminobenzamidine- and Benzamidine-Viia/Soluble Tissue Factor: Unpredicted Conformation of the 192-193 Peptide Bond and Mapping of CA2+, MG2+, Na+ and ZN2+ Sites in Factor Viia J.Biol.Chem. V. 281 24873 2006.
ISSN: ISSN 0021-9258
PubMed: 16757484
DOI: 10.1074/JBC.M509971200
Page generated: Thu Oct 29 04:07:23 2020

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