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Calcium in PDB 1g3d: Bovine Beta-Trypsin Bound to Meta-Amidino Schiff Base Copper (II) Chelate

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

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

Protein crystallography data

The structure of Bovine Beta-Trypsin Bound to Meta-Amidino Schiff Base Copper (II) Chelate, PDB code: 1g3d 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) 19.36 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.810, 63.260, 69.250, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 18.9

Other elements in 1g3d:

The structure of Bovine Beta-Trypsin Bound to Meta-Amidino 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-Amidino Schiff Base Copper (II) Chelate (pdb code 1g3d). 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 Copper (II) Chelate, PDB code: 1g3d:

Calcium binding site 1 out of 1 in 1g3d

Go back to Calcium Binding Sites List in 1g3d
Calcium binding site 1 out of 1 in the Bovine Beta-Trypsin Bound to Meta-Amidino 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-Amidino Schiff Base Copper (II) Chelate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca502

b:18.1
occ:1.00
 OE1 A:GLU70 2.2 13.9 1.0
O A:VAL75 2.2 14.2 1.0
OE2 A:GLU80 2.2 12.3 1.0
O A:HOH845 2.3 12.1 1.0
O A:HOH774 2.3 13.7 1.0
O A:ASN72 2.3 11.7 1.0
CD A:GLU70 3.2 14.7 1.0
CD A:GLU80 3.3 13.9 1.0
C A:VAL75 3.3 14.9 1.0
C A:ASN72 3.4 13.5 1.0
OE2 A:GLU70 3.6 16.0 1.0
CG A:GLU80 3.7 14.2 1.0
CA A:VAL76 4.0 15.0 1.0
N A:GLU77 4.1 15.9 1.0
N A:VAL76 4.1 14.2 1.0
CA A:ILE73 4.2 13.8 1.0
N A:VAL75 4.2 14.7 1.0
N A:ILE73 4.3 12.8 1.0
OE1 A:GLU77 4.3 17.1 1.0
N A:ASN72 4.3 13.4 1.0
O A:HOH773 4.3 14.2 1.0
CA A:VAL75 4.4 15.2 1.0
OE1 A:GLU80 4.4 12.9 1.0
CA A:ASN72 4.4 13.1 1.0
CG A:GLU77 4.5 17.5 1.0
C A:ILE73 4.5 14.0 1.0
CG A:GLU70 4.5 12.0 1.0
C A:VAL76 4.6 16.1 1.0
O A:HOH846 4.6 24.1 1.0
N A:ASP71 4.6 12.9 1.0
CB A:ASN72 4.7 14.5 1.0
N A:ASN74 4.8 14.7 1.0
CA A:GLU70 4.8 11.7 1.0
CB A:GLU70 4.8 12.3 1.0
CD A:GLU77 4.9 19.6 1.0
CB A:GLU77 4.9 16.8 1.0
O A:ILE73 4.9 13.6 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 08:29:13 2024

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