Atomistry » Calcium » PDB 4niv-4o4h » 4niw
Atomistry »
  Calcium »
    PDB 4niv-4o4h »
      4niw »

Calcium in PDB 4niw: Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form

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

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

Protein crystallography data

The structure of Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form, PDB code: 4niw 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) 44.06 / 1.31
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.522, 58.607, 66.831, 90.00, 90.00, 90.00
R / Rfree (%) 12.8 / 15.5

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Trypsiligase (K60E/N143H/Y151H/D189K Trypsin) Orthorhombic Form (pdb code 4niw). 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, PDB code: 4niw:

Calcium binding site 1 out of 1 in 4niw

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


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 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca301

b:6.2
occ:1.00
OE1 A:GLU70 2.3 7.2 1.0
O A:VAL75 2.3 6.8 1.0
OE2 A:GLU80 2.4 7.9 1.0
O A:ASN72 2.4 6.6 1.0
O A:HOH418 2.4 8.3 1.0
O A:HOH404 2.4 7.7 1.0
CD A:GLU70 3.4 6.2 1.0
CD A:GLU80 3.4 7.3 1.0
C A:VAL75 3.4 6.5 1.0
C A:ASN72 3.5 5.9 1.0
OE2 A:GLU70 3.8 7.0 1.0
CG A:GLU80 3.8 8.9 1.0
CA A:VAL76 4.1 7.6 1.0
N A:GLU77 4.2 7.8 1.0
N A:VAL76 4.2 6.8 1.0
N A:VAL75 4.2 6.3 1.0
OE1 A:GLU77 4.2 8.8 1.0
CA A:ILE73 4.3 6.2 1.0
N A:ILE73 4.4 5.4 1.0
N A:ASN72 4.4 6.5 1.0
CA A:VAL75 4.4 6.5 1.0
CA A:ASN72 4.5 6.3 1.0
O A:HOH403 4.5 8.8 1.0
CG A:GLU77 4.5 9.2 1.0
N A:ASP71 4.5 7.3 1.0
C A:ILE73 4.5 5.6 1.0
OE1 A:GLU80 4.5 8.4 1.0
C A:VAL76 4.6 8.1 1.0
CG A:GLU70 4.7 6.7 1.0
CA A:GLU70 4.7 6.7 1.0
CD A:GLU77 4.8 9.9 1.0
CB A:GLU77 4.8 8.7 1.0
CB A:GLU70 4.8 5.9 1.0
N A:ASN74 4.9 5.4 1.0
O A:HOH438 4.9 13.4 1.0
O A:ILE73 4.9 6.4 1.0
CB A:ASN72 4.9 7.2 1.0
C A:ASP71 5.0 6.8 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

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy