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Magnesium in PDB 1s6h: Porcine Trypsin Complexed with Guanidine-3-Propanol Inhibitor

Enzymatic activity of Porcine Trypsin Complexed with Guanidine-3-Propanol Inhibitor

All present enzymatic activity of Porcine Trypsin Complexed with Guanidine-3-Propanol Inhibitor:
3.4.21.4;

Protein crystallography data

The structure of Porcine Trypsin Complexed with Guanidine-3-Propanol Inhibitor, PDB code: 1s6h was solved by T.R.Transue, J.M.Krahn, S.A.Gabel, E.F.Derose, R.E.London, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 100.00 / 1.45
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 76.228, 53.198, 46.515, 90.00, 90.00, 90.00
R / Rfree (%) 15.4 / 17.9

Other elements in 1s6h:

The structure of Porcine Trypsin Complexed with Guanidine-3-Propanol Inhibitor also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Porcine Trypsin Complexed with Guanidine-3-Propanol Inhibitor (pdb code 1s6h). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Porcine Trypsin Complexed with Guanidine-3-Propanol Inhibitor, PDB code: 1s6h:

Magnesium binding site 1 out of 1 in 1s6h

Go back to Magnesium Binding Sites List in 1s6h
Magnesium binding site 1 out of 1 in the Porcine Trypsin Complexed with Guanidine-3-Propanol Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Porcine Trypsin Complexed with Guanidine-3-Propanol Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg5

b:29.2
occ:0.77
H2 A:HOH433 1.6 21.1 0.9
H2 A:HOH436 1.9 25.2 0.8
H1 A:HOH437 1.9 35.7 1.0
O A:HOH433 2.0 21.1 0.9
O A:HOH436 2.1 25.2 0.8
O A:HOH437 2.1 35.7 1.0
O A:HOH434 2.3 29.3 0.8
H1 A:HOH434 2.3 29.3 0.8
O A:HOH438 2.4 34.1 0.8
O A:HOH435 2.4 25.4 1.0
H1 A:HOH436 2.5 25.2 0.8
H2 A:HOH434 2.5 29.3 0.8
H1 A:HOH438 2.5 34.1 0.8
H1 A:HOH433 2.8 21.1 0.9
H1 A:HOH435 2.9 25.4 1.0
H2 A:HOH435 2.9 25.4 1.0
H2 A:HOH437 3.0 35.7 1.0
H2 A:HOH438 3.1 34.1 0.8
H1 A:HOH429 3.6 18.0 0.7
OD2 A:ASP74 4.0 17.4 1.0
H2 A:HOH529 4.1 20.9 0.6
H2 A:HOH429 4.1 18.0 0.7
O A:TYR151 4.1 15.2 1.0
HB2 A:TYR151 4.2 15.0 1.0
O A:HOH529 4.2 20.9 0.6
O A:HOH429 4.3 18.0 0.7
O A:HOH492 4.3 29.6 0.8
OD1 A:ASP74 4.3 18.1 1.0
H1 A:HOH342 4.4 12.7 0.8
HG A:SER153 4.4 11.1 0.5
CG A:ASP74 4.5 16.8 1.0
O A:HOH487 4.5 40.0 0.8
H1 A:HOH465 4.6 24.3 0.6
HB3 A:TYR151 4.6 15.0 1.0
H1 A:HOH446 4.6 27.9 0.9
H2 A:HOH492 4.8 29.6 0.8
CB A:TYR151 4.9 15.0 1.0
H1 A:HOH492 4.9 29.6 0.8
H1 A:HOH529 5.0 20.9 0.6
H1 A:HOH487 5.0 40.0 0.8

Reference:

T.R.Transue, J.M.Krahn, S.A.Gabel, E.F.Derose, R.E.London. X-Ray and uc(Nmr) Characterization of Covalent Complexes of Trypsin, Borate, and Alcohols. Biochemistry V. 43 2829 2004.
ISSN: ISSN 0006-2960
PubMed: 15005618
DOI: 10.1021/BI035782Y
Page generated: Tue Aug 13 13:16:23 2024

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