Atomistry » Calcium » PDB 3a4u-3aas » 3aas
Atomistry »
  Calcium »
    PDB 3a4u-3aas »
      3aas »

Calcium in PDB 3aas: Bovine Beta-Trypsin Bound to Meta-Guanidino Schiff Base Copper (II) Chelate

Enzymatic activity of Bovine Beta-Trypsin Bound to Meta-Guanidino Schiff Base Copper (II) Chelate

All present enzymatic activity of Bovine Beta-Trypsin Bound to Meta-Guanidino Schiff Base Copper (II) Chelate:
3.4.21.4;

Protein crystallography data

The structure of Bovine Beta-Trypsin Bound to Meta-Guanidino Schiff Base Copper (II) Chelate, PDB code: 3aas was solved by D.Iyaguchi, S.Kawano, E.Toyota, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.75
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.990, 56.295, 65.742, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 20.9

Other elements in 3aas:

The structure of Bovine Beta-Trypsin Bound to Meta-Guanidino Schiff Base Copper (II) Chelate also contains other interesting chemical elements:

Copper (Cu) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Bovine Beta-Trypsin Bound to Meta-Guanidino Schiff Base Copper (II) Chelate (pdb code 3aas). 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 Bovine Beta-Trypsin Bound to Meta-Guanidino Schiff Base Copper (II) Chelate, PDB code: 3aas:

Calcium binding site 1 out of 1 in 3aas

Go back to Calcium Binding Sites List in 3aas
Calcium binding site 1 out of 1 in the Bovine Beta-Trypsin Bound to Meta-Guanidino Schiff Base Copper (II) Chelate


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Bovine Beta-Trypsin Bound to Meta-Guanidino Schiff Base Copper (II) Chelate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca2001

b:16.4
occ:1.00
 OE1 A:GLU52 2.2 15.7 1.0
O A:VAL57 2.2 15.8 1.0
O A:HOH401 2.3 16.8 1.0
OE2 A:GLU62 2.4 17.7 1.0
O A:ASN54 2.4 15.2 1.0
O A:HOH291 2.5 16.9 1.0
CD A:GLU52 3.3 16.7 1.0
C A:VAL57 3.4 14.5 1.0
CD A:GLU62 3.4 17.4 1.0
C A:ASN54 3.5 17.4 1.0
OE2 A:GLU52 3.7 15.6 1.0
CG A:GLU62 3.7 17.7 1.0
CA A:VAL58 4.1 17.1 1.0
N A:GLU59 4.1 17.6 1.0
N A:VAL58 4.1 16.4 1.0
N A:VAL57 4.2 14.7 1.0
CA A:ILE55 4.2 16.7 1.0
OE1 A:GLU59 4.2 18.2 1.0
N A:ILE55 4.3 17.4 1.0
CA A:VAL57 4.3 15.3 1.0
N A:ASN54 4.4 17.3 1.0
C A:ILE55 4.5 15.7 1.0
CA A:ASN54 4.5 16.4 1.0
OE1 A:GLU62 4.5 16.3 1.0
CG A:GLU59 4.5 17.4 1.0
O A:HOH288 4.6 18.8 1.0
CG A:GLU52 4.6 16.3 1.0
N A:ASP53 4.6 16.8 1.0
C A:VAL58 4.6 18.1 1.0
CA A:GLU52 4.8 15.5 1.0
CD A:GLU59 4.8 21.4 1.0
CB A:GLU59 4.8 17.9 1.0
N A:ASN56 4.8 15.2 1.0
CB A:GLU52 4.8 17.0 1.0
CB A:ASN54 4.9 18.0 1.0
O A:ILE55 4.9 16.1 1.0

Reference:

D.Iyaguchi, S.Kawano, K.Takada, E.Toyota. Structural Basis For the Design of Novel Schiff Base Metal Chelate Inhibitors of Trypsin Bioorg.Med.Chem. V. 18 2076 2010.
ISSN: ISSN 0968-0896
PubMed: 20202854
DOI: 10.1016/J.BMC.2010.02.016
Page generated: Sat Jul 13 07:20:09 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy