Calcium in PDB 4b2c: Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tpa) in Complex with Eglin C

All present enzymatic activity of Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tpa) in Complex with Eglin C:
3.4.21.4;

The structure of Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tpa) in Complex with Eglin C, PDB code: 4b2c was solved by A.Menzel, P.Neumann, M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.43
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	79.210, 37.020, 103.960, 90.00, 102.26, 90.00
R / Rfree (%)	15.8 / 18.2

The structure of Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tpa) in Complex with Eglin C also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Calcium atom in the Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tpa) in Complex with Eglin C (pdb code 4b2c). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tpa) in Complex with Eglin C, PDB code: 4b2c:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tpa) in Complex with Eglin C


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tpa) in Complex with Eglin C within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1246 b:11.0 occ:1.00 OE2 A:GLU80 2.3 11.2 1.0 O A:ASN72 2.3 11.2 1.0 OE1 A:GLU70 2.3 12.1 1.0 O A:VAL75 2.3 11.9 1.0 O A:HOH2070 2.4 12.4 1.0 O A:HOH2069 2.4 12.1 1.0 CD A:GLU70 3.4 12.0 1.0 CD A:GLU80 3.4 12.0 1.0 C A:VAL75 3.5 11.9 1.0 C A:ASN72 3.5 11.4 1.0 CG A:GLU80 3.7 12.5 1.0 OE2 A:GLU70 3.8 12.9 1.0 N A:GLU77 4.1 12.7 1.0 CA A:VAL76 4.2 12.3 1.0 N A:VAL76 4.2 12.1 1.0 CA A:ILE73 4.2 10.7 1.0 OE1 A:GLU77 4.3 14.2 1.0 N A:VAL75 4.3 11.7 1.0 N A:ILE73 4.3 11.0 1.0 N A:ASN72 4.4 11.9 1.0 CA A:ASN72 4.4 11.5 1.0 CG A:GLU77 4.5 15.7 1.0 C A:ILE73 4.5 11.5 1.0 O A:HOH2068 4.5 12.6 1.0 CA A:VAL75 4.5 12.2 1.0 OE1 A:GLU80 4.5 13.0 1.0 N A:ASP71 4.6 11.8 1.0 C A:VAL76 4.6 12.8 1.0 CG A:GLU70 4.7 11.8 1.0 CB A:ASN72 4.7 12.9 1.0 O A:HOH2075 4.7 23.9 1.0 CA A:GLU70 4.8 11.7 1.0 CD A:GLU77 4.8 17.4 1.0 N A:ASN74 4.8 10.7 1.0 CB A:GLU77 4.8 14.5 1.0 O A:ILE73 4.9 11.7 1.0 CB A:GLU70 4.9 12.0 1.0 C A:ASP71 5.0 11.4 1.0

Calcium binding site 2 out of 2 in the Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tpa) in Complex with Eglin C


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tpa) in Complex with Eglin C within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca1246 b:11.9 occ:1.00 OE1 C:GLU70 2.2 12.6 1.0 OE2 C:GLU80 2.3 13.8 1.0 O C:VAL75 2.3 13.7 1.0 O C:ASN72 2.3 14.1 1.0 O C:HOH2067 2.4 13.5 1.0 O C:HOH2066 2.4 15.0 1.0 CD C:GLU70 3.3 12.5 1.0 CD C:GLU80 3.4 13.6 1.0 C C:VAL75 3.5 13.5 1.0 C C:ASN72 3.5 12.2 1.0 OE2 C:GLU70 3.7 12.3 1.0 CG C:GLU80 3.7 13.4 1.0 CA C:VAL76 4.1 14.0 1.0 N C:GLU77 4.1 14.3 1.0 N C:VAL76 4.2 13.9 1.0 OE1 C:GLU77 4.3 15.7 1.0 CA C:ILE73 4.3 12.3 1.0 N C:VAL75 4.3 13.9 1.0 N C:ILE73 4.3 12.1 1.0 N C:ASN72 4.4 11.6 1.0 CG C:GLU77 4.4 16.3 1.0 CA C:ASN72 4.4 11.4 1.0 O C:HOH2065 4.5 12.9 1.0 OE1 C:GLU80 4.5 13.9 1.0 C C:ILE73 4.5 12.9 1.0 CA C:VAL75 4.5 13.8 1.0 N C:ASP71 4.6 12.4 1.0 C C:VAL76 4.6 14.5 1.0 CG C:GLU70 4.6 11.8 1.0 CA C:GLU70 4.7 11.7 1.0 CB C:GLU77 4.7 15.4 1.0 CB C:ASN72 4.8 12.8 1.0 CD C:GLU77 4.8 17.2 1.0 O C:HOH2039 4.8 25.5 1.0 CB C:GLU70 4.8 12.0 1.0 N C:ASN74 4.8 11.7 1.0 O C:ILE73 4.9 12.9 1.0 C C:ASP71 5.0 12.4 1.0

A.Menzel, P.Neumann, C.Schwieger, M.T.Stubbs. Thermodynamic Signatures in Macromolecular Interactions Involving Conformational Flexibility. Biol.Chem. V. 395 905 2014.
ISSN: ISSN 1431-6730
PubMed: 25003391
DOI: 10.1515/HSZ-2014-0177