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Calcium in PDB 4nix: Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form, Zinc-Bound

Enzymatic activity of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form, Zinc-Bound

All present enzymatic activity of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form, Zinc-Bound:
3.4.21.4;

Protein crystallography data

The structure of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form, Zinc-Bound, PDB code: 4nix was solved by M.Schoepfel, C.Parthier, M.T.Stubbs, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 44.18 / 1.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.404, 58.550, 67.316, 90.00, 90.00, 90.00
R / Rfree (%) 13 / 15.7

Other elements in 4nix:

The structure of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form, Zinc-Bound also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form, Zinc-Bound (pdb code 4nix). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form, Zinc-Bound, PDB code: 4nix:

Calcium binding site 1 out of 1 in 4nix

Go back to Calcium Binding Sites List in 4nix
Calcium binding site 1 out of 1 in the Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form, Zinc-Bound


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form, Zinc-Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:7.2
occ:0.48
 O A:VAL75 2.1 11.7 1.0
O A:HOH652 2.2 12.1 1.0
OE1 A:GLU70 2.2 11.4 1.0
O A:ASN72 2.5 8.1 1.0
O A:HOH449 2.5 16.9 1.0
OE2 A:GLU80 2.5 12.5 1.0
C A:VAL75 3.3 9.3 1.0
CD A:GLU70 3.3 9.0 1.0
CD A:GLU80 3.6 9.3 1.0
C A:ASN72 3.6 7.7 1.0
OE2 A:GLU70 3.7 10.9 1.0
CG A:GLU80 3.9 10.3 1.0
CA A:VAL76 4.0 9.5 1.0
N A:VAL76 4.1 8.7 1.0
OE1 A:GLU77 4.1 12.4 1.0
N A:VAL75 4.1 7.6 1.0
N A:GLU77 4.1 9.2 1.0
CA A:VAL75 4.3 8.5 1.0
N A:ASN72 4.4 6.9 1.0
CA A:ILE73 4.4 7.7 1.0
N A:ASP71 4.4 7.4 1.0
N A:ILE73 4.5 6.9 1.0
CG A:GLU77 4.5 10.3 1.0
CG A:GLU70 4.5 8.5 1.0
CA A:ASN72 4.5 7.3 1.0
C A:ILE73 4.6 7.2 1.0
C A:VAL76 4.6 9.9 1.0
CA A:GLU70 4.6 7.6 1.0
OE1 A:GLU80 4.7 9.3 1.0
CB A:GLU70 4.7 8.2 1.0
CD A:GLU77 4.7 12.7 1.0
O A:HOH427 4.7 12.6 1.0
CB A:GLU77 4.8 9.8 1.0
O A:ILE73 4.8 8.4 1.0
CB A:VAL75 4.9 10.5 1.0
N A:ASN74 4.9 6.5 1.0

Reference:

S.Liebscher, M.Schopfel, T.Aumuller, A.Sharkhuukhen, A.Pech, E.Hoss, C.Parthier, G.Jahreis, M.T.Stubbs, F.Bordusa. N-Terminal Protein Modification By Substrate-Activated Reverse Proteolysis. Angew.Chem.Int.Ed.Engl. V. 53 3024 2014.
ISSN: ISSN 1433-7851
PubMed: 24520050
DOI: 10.1002/ANIE.201307736
Page generated: Sat Dec 12 05:01:10 2020

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