Arsenic in PDB 4zma: Crystal Structure of A Fviia-Trypsin Chimera (St) in Complex with Soluble Tissue Factor

All present enzymatic activity of Crystal Structure of A Fviia-Trypsin Chimera (St) in Complex with Soluble Tissue Factor:
3.4.21.21;

The structure of Crystal Structure of A Fviia-Trypsin Chimera (St) in Complex with Soluble Tissue Factor, PDB code: 4zma was solved by A.B.Sorensen, L.A.Svensson, P.S.Gandhi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.77 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	66.209, 80.898, 125.759, 90.00, 90.00, 90.00
R / Rfree (%)	24 / 29.5

The structure of Crystal Structure of A Fviia-Trypsin Chimera (St) in Complex with Soluble Tissue Factor also contains other interesting chemical elements:

Calcium

(Ca)

8 atoms

The binding sites of Arsenic atom in the Crystal Structure of A Fviia-Trypsin Chimera (St) in Complex with Soluble Tissue Factor (pdb code 4zma). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 2 binding sites of Arsenic where determined in the Crystal Structure of A Fviia-Trypsin Chimera (St) in Complex with Soluble Tissue Factor, PDB code: 4zma:
Jump to Arsenic binding site number: 1; 2;

Arsenic binding site 1 out of 2 in the Crystal Structure of A Fviia-Trypsin Chimera (St) in Complex with Soluble Tissue Factor


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of A Fviia-Trypsin Chimera (St) in Complex with Soluble Tissue Factor within 5.0Å range: probe atom residue distance (Å) B Occ H:As503 b:81.3 occ:1.00 AS H:CAC503 0.0 81.3 1.0 O2 H:CAC503 1.7 50.0 1.0 O1 H:CAC503 1.7 57.4 1.0 C2 H:CAC503 2.0 46.8 1.0 C1 H:CAC503 2.0 53.4 1.0 ND1 H:HIS224 3.0 47.7 1.0 H H:PHE225 3.5 39.2 1.0 HG H:SER171 3.5 65.6 1.0 OE1 H:GLN217 3.6 54.3 1.0 HA H:HIS224 3.7 44.6 1.0 HB3 H:HIS224 3.7 46.6 1.0 CE1 H:HIS224 3.9 53.7 1.0 HE1 H:HIS224 3.9 64.4 1.0 HB2 H:SER171 4.0 65.9 1.0 CG H:HIS224 4.0 44.5 1.0 OG H:SER171 4.2 54.6 1.0 HD11 H:ILE176 4.2 47.9 1.0 CB H:HIS224 4.2 38.8 1.0 HG H:CYS182 4.3 34.7 0.7 N H:PHE225 4.3 32.7 1.0 CA H:HIS224 4.4 37.2 1.0 HG3 H:GLN217 4.4 53.0 1.0 O H:PHE225 4.4 32.6 1.0 CD H:GLN217 4.5 50.9 1.0 CB H:SER171 4.5 54.9 1.0 HB2 H:GLN217 4.7 45.5 1.0 HB3 H:SER171 4.7 65.9 1.0 HD2 H:PHE225 4.7 41.8 1.0 SG H:CYS168 4.8 40.4 0.6 O H:CYS168 4.9 36.3 1.0 C H:HIS224 4.9 35.2 1.0 CG H:GLN217 4.9 44.2 1.0 HG22 H:VAL227 5.0 24.5 1.0

Arsenic binding site 2 out of 2 in the Crystal Structure of A Fviia-Trypsin Chimera (St) in Complex with Soluble Tissue Factor


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of Crystal Structure of A Fviia-Trypsin Chimera (St) in Complex with Soluble Tissue Factor within 5.0Å range: probe atom residue distance (Å) B Occ H:As504 b:67.2 occ:1.00 AS H:CAC504 0.0 67.2 1.0 O2 H:CAC504 1.7 62.0 1.0 O1 H:CAC504 1.7 47.6 1.0 C1 H:CAC504 2.0 52.3 1.0 C2 H:CAC504 2.0 66.5 1.0 OE2 H:GLU26 3.4 48.0 1.0 HG2 H:PRO23 3.9 46.9 1.0 OE1 H:GLU26 3.9 41.1 1.0 CD H:GLU26 4.1 44.0 1.0 O H:HOH673 4.2 44.1 1.0 CG H:PRO23 4.8 39.0 1.0 HG3 H:PRO23 5.0 46.9 1.0

A.B.Sorensen, J.J.Madsen, L.A.Svensson, A.A.Pedersen, H.Stergaard, M.T.Overgaard, O.H.Olsen, P.S.Gandhi. Molecular Basis of Enhanced Activity in Factor Viia-Trypsin Variants Conveys Insights Into Tissue Factor-Mediated Allosteric Regulation of Factor Viia Activity. J.Biol.Chem. V. 291 4671 2016.
ISSN: ESSN 1083-351X
PubMed: 26694616
DOI: 10.1074/JBC.M115.698613