Calcium in PDB 4b2b: Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tgpa) in Complex with Eglin C

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

The structure of Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tgpa) in Complex with Eglin C, PDB code: 4b2b 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 / 1.36
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	78.340, 36.940, 103.020, 90.00, 103.41, 90.00
R / Rfree (%)	18.3 / 20.4

The structure of Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tgpa) 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 (Tgpa) in Complex with Eglin C (pdb code 4b2b). 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 (Tgpa) in Complex with Eglin C, PDB code: 4b2b:
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 (Tgpa) 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 (Tgpa) in Complex with Eglin C within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1246 b:9.5 occ:1.00 OE1 A:GLU70 2.2 10.9 1.0 O A:ASN72 2.3 10.4 1.0 O A:VAL75 2.3 9.4 1.0 O A:HOH2067 2.3 12.4 1.0 OE2 A:GLU80 2.4 10.0 1.0 O A:HOH2068 2.4 10.5 1.0 CD A:GLU70 3.3 10.9 1.0 C A:VAL75 3.4 9.7 1.0 CD A:GLU80 3.5 10.7 1.0 C A:ASN72 3.5 10.2 1.0 CG A:GLU80 3.7 10.6 1.0 OE2 A:GLU70 3.7 10.6 1.0 N A:GLU77 4.1 10.6 1.0 CA A:VAL76 4.1 10.4 1.0 N A:VAL76 4.2 10.1 1.0 OE1 A:GLU77 4.3 11.7 1.0 CA A:ILE73 4.3 10.8 1.0 N A:VAL75 4.3 10.2 1.0 N A:ILE73 4.3 10.7 1.0 N A:ASN72 4.4 10.6 1.0 CA A:ASN72 4.4 10.2 1.0 CG A:GLU77 4.4 12.8 1.0 C A:ILE73 4.5 10.8 1.0 CA A:VAL75 4.5 10.2 1.0 O A:HOH2066 4.5 12.4 1.0 OE1 A:GLU80 4.6 10.3 1.0 N A:ASP71 4.6 10.3 1.0 CG A:GLU70 4.6 10.4 1.0 C A:VAL76 4.6 10.5 1.0 CB A:ASN72 4.7 11.1 1.0 O A:HOH2074 4.7 19.8 1.0 CB A:GLU77 4.7 12.1 1.0 CD A:GLU77 4.8 13.6 1.0 N A:ASN74 4.8 9.7 1.0 CA A:GLU70 4.8 10.1 1.0 O A:ILE73 4.9 10.7 1.0 CB A:GLU70 4.9 10.6 1.0 C A:ASP71 5.0 10.6 1.0

Calcium binding site 2 out of 2 in the Structure of the Factor Xa-Like Trypsin Variant Triple-Ala (Tgpa) 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 (Tgpa) in Complex with Eglin C within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca1246 b:7.9 occ:1.00 OE1 C:GLU70 2.3 8.2 1.0 O C:VAL75 2.3 8.4 1.0 O C:ASN72 2.4 9.5 1.0 OE2 C:GLU80 2.4 10.2 1.0 O C:HOH2083 2.4 7.5 1.0 O C:HOH2082 2.4 9.9 1.0 CD C:GLU70 3.4 8.0 1.0 CD C:GLU80 3.5 9.4 1.0 C C:VAL75 3.5 9.1 1.0 C C:ASN72 3.5 8.7 1.0 OE2 C:GLU70 3.8 8.9 1.0 CG C:GLU80 3.8 9.7 1.0 N C:GLU77 4.1 9.3 1.0 CA C:VAL76 4.1 9.4 1.0 OE1 C:GLU77 4.2 9.9 1.0 N C:VAL76 4.2 9.6 1.0 N C:VAL75 4.3 8.8 1.0 N C:ASN72 4.3 8.4 1.0 CA C:ILE73 4.3 8.1 1.0 N C:ILE73 4.4 7.9 1.0 CA C:ASN72 4.4 8.4 1.0 O C:HOH2081 4.5 9.1 1.0 CG C:GLU77 4.5 9.9 1.0 C C:ILE73 4.5 9.8 1.0 OE1 C:GLU80 4.5 9.5 1.0 CA C:VAL75 4.6 9.3 1.0 N C:ASP71 4.6 9.1 1.0 C C:VAL76 4.6 9.7 1.0 CG C:GLU70 4.6 7.5 1.0 CB C:ASN72 4.7 8.9 1.0 CD C:GLU77 4.7 11.2 1.0 CA C:GLU70 4.8 7.9 1.0 CB C:GLU77 4.8 9.9 1.0 O C:HOH2089 4.8 19.8 1.0 N C:ASN74 4.8 9.1 1.0 CB C:GLU70 4.9 7.7 1.0 O C:ILE73 4.9 8.5 1.0 C C:ASP71 5.0 9.1 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