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Calcium in PDB 7q0w: Bovine Trypsin Co-Crystallized with V(IV)OSO4 and Phen

Enzymatic activity of Bovine Trypsin Co-Crystallized with V(IV)OSO4 and Phen

All present enzymatic activity of Bovine Trypsin Co-Crystallized with V(IV)OSO4 and Phen:
3.4.21.4;

Protein crystallography data

The structure of Bovine Trypsin Co-Crystallized with V(IV)OSO4 and Phen, PDB code: 7q0w was solved by M.F.A.Santos, A.C.P.Fernandes, I.Correia, G.Sciortino, E.Garribba, T.Santos-Silva, J.C.Pessoa, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.68 / 1.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 53.905, 56.082, 65.779, 90, 90, 90
R / Rfree (%) 12.7 / 16.2

Other elements in 7q0w:

The structure of Bovine Trypsin Co-Crystallized with V(IV)OSO4 and Phen also contains other interesting chemical elements:

Vanadium (V) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Bovine Trypsin Co-Crystallized with V(IV)OSO4 and Phen (pdb code 7q0w). 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 Trypsin Co-Crystallized with V(IV)OSO4 and Phen, PDB code: 7q0w:

Calcium binding site 1 out of 1 in 7q0w

Go back to Calcium Binding Sites List in 7q0w
Calcium binding site 1 out of 1 in the Bovine Trypsin Co-Crystallized with V(IV)OSO4 and Phen


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Bovine Trypsin Co-Crystallized with V(IV)OSO4 and Phen within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca305

b:10.7
occ:1.00
OE1 A:GLU70 2.3 10.7 1.0
O A:VAL75 2.3 11.0 1.0
O A:ASN72 2.3 10.4 1.0
OE2 A:GLU80 2.3 11.9 1.0
O A:HOH473 2.3 12.4 1.0
O A:HOH405 2.4 11.8 1.0
CD A:GLU70 3.4 10.1 1.0
CD A:GLU80 3.4 12.0 1.0
C A:VAL75 3.4 10.5 1.0
C A:ASN72 3.5 9.8 1.0
CG A:GLU80 3.7 13.4 1.0
OE2 A:GLU70 3.8 11.1 1.0
CA A:VAL76 4.1 13.3 1.0
N A:GLU77 4.2 13.0 1.0
N A:VAL76 4.2 11.6 1.0
N A:VAL75 4.2 10.5 1.0
CA A:ILE73 4.2 10.9 1.0
OE1 A:GLU77 4.3 13.6 1.0
N A:ILE73 4.3 10.1 1.0
N A:ASN72 4.4 10.6 1.0
CA A:VAL75 4.4 10.7 1.0
CA A:ASN72 4.4 10.2 1.0
O A:HOH460 4.5 13.5 1.0
CG A:GLU77 4.5 13.0 1.0
OE1 A:GLU80 4.5 13.2 1.0
C A:ILE73 4.5 9.7 1.0
N A:ASP71 4.5 10.6 1.0
CG A:GLU70 4.6 10.9 1.0
C A:VAL76 4.7 13.2 1.0
CA A:GLU70 4.7 9.9 1.0
CB A:GLU77 4.8 14.3 1.0
CD A:GLU77 4.8 14.3 1.0
CB A:GLU70 4.8 10.2 1.0
CB A:ASN72 4.9 11.1 1.0
N A:ASN74 4.9 9.8 1.0
O A:HOH582 4.9 28.6 1.0
O A:ILE73 5.0 11.6 1.0
C A:ASP71 5.0 10.4 1.0

Reference:

M.F.A.Santos, G.Sciortino, I.Correia, A.C.P.Fernandes, T.Santos-Silva, F.Pisanu, E.Garribba, J.Costa Pessoa. Binding of V IV O 2+ , V IV Ol, V IV Ol 2 and V V O 2 L Moieties to Proteins: X-Ray/Theoretical Characterization and Biological Implications. Chemistry V. 28 00105 2022.
ISSN: ISSN 0947-6539
PubMed: 35486702
DOI: 10.1002/CHEM.202200105
Page generated: Fri Jul 19 03:22:51 2024

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