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Calcium in PDB 1g3b: Bovine Beta-Trypsin Bound to Meta-Amidino Schiff Base Magnesium(II) Chelate

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

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

Protein crystallography data

The structure of Bovine Beta-Trypsin Bound to Meta-Amidino Schiff Base Magnesium(II) Chelate, PDB code: 1g3b was solved by E.Toyota, K.K.S.Ng, H.Sekizaki, K.Itoh, K.Tanizawa, M.N.G.James, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.35 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.770, 63.250, 69.330, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 19.3

Other elements in 1g3b:

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

Magnesium (Mg) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Bovine Beta-Trypsin Bound to Meta-Amidino Schiff Base Magnesium(II) Chelate (pdb code 1g3b). 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-Amidino Schiff Base Magnesium(II) Chelate, PDB code: 1g3b:

Calcium binding site 1 out of 1 in 1g3b

Go back to Calcium Binding Sites List in 1g3b
Calcium binding site 1 out of 1 in the Bovine Beta-Trypsin Bound to Meta-Amidino Schiff Base Magnesium(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-Amidino Schiff Base Magnesium(II) Chelate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca502

b:16.5
occ:1.00
 OE1 A:GLU70 2.2 11.4 1.0
O A:VAL75 2.2 13.4 1.0
OE2 A:GLU80 2.2 11.3 1.0
O A:HOH739 2.3 11.2 1.0
O A:HOH737 2.3 11.6 1.0
O A:ASN72 2.3 11.5 1.0
CD A:GLU70 3.3 12.7 1.0
CD A:GLU80 3.3 10.9 1.0
C A:VAL75 3.4 13.3 1.0
C A:ASN72 3.4 11.7 1.0
OE2 A:GLU70 3.7 12.0 1.0
CG A:GLU80 3.7 11.7 1.0
CA A:VAL76 4.0 13.3 1.0
N A:GLU77 4.1 13.6 1.0
N A:VAL76 4.1 11.8 1.0
CA A:ILE73 4.2 12.5 1.0
N A:VAL75 4.2 13.7 1.0
N A:ILE73 4.3 11.4 1.0
OE1 A:GLU77 4.3 14.4 1.0
N A:ASN72 4.3 11.7 1.0
O A:HOH740 4.3 14.6 1.0
CA A:VAL75 4.4 14.3 1.0
CA A:ASN72 4.4 12.0 1.0
OE1 A:GLU80 4.4 12.0 1.0
C A:ILE73 4.5 12.6 1.0
CG A:GLU77 4.5 15.9 1.0
CG A:GLU70 4.6 10.7 1.0
N A:ASP71 4.6 12.3 1.0
C A:VAL76 4.6 13.7 1.0
O A:HOH738 4.7 18.3 1.0
CB A:ASN72 4.7 14.1 1.0
CA A:GLU70 4.8 11.2 1.0
CB A:GLU70 4.8 11.2 1.0
N A:ASN74 4.9 13.7 1.0
CB A:GLU77 4.9 14.3 1.0
CD A:GLU77 4.9 17.1 1.0
O A:ILE73 5.0 11.9 1.0

Reference:

E.Toyota, K.K.Ng, H.Sekizaki, K.Itoh, K.Tanizawa, M.N.James. X-Ray Crystallographic Analyses of Complexes Between Bovine Beta-Trypsin and Schiff Base Copper(II) or Iron(III) Chelates. J.Mol.Biol. V. 305 471 2001.
ISSN: ISSN 0022-2836
PubMed: 11152605
DOI: 10.1006/JMBI.2000.4303
Page generated: Thu Jul 11 08:29:06 2024

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