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Chlorine in PDB 2bza: Bovine Pancreas Beta-Trypsin in Complex with Benzylamine

Enzymatic activity of Bovine Pancreas Beta-Trypsin in Complex with Benzylamine

All present enzymatic activity of Bovine Pancreas Beta-Trypsin in Complex with Benzylamine:
3.4.21.4;

Protein crystallography data

The structure of Bovine Pancreas Beta-Trypsin in Complex with Benzylamine, PDB code: 2bza was solved by N.Ota, C.Stroupe, J.M.S.Ferreira-Da-Silva, S.S.Shah, M.Mares-Guia, A.T.Brunger, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 32.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 63.401, 63.722, 69.174, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 19.5

Other elements in 2bza:

The structure of Bovine Pancreas Beta-Trypsin in Complex with Benzylamine also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Bovine Pancreas Beta-Trypsin in Complex with Benzylamine (pdb code 2bza). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Bovine Pancreas Beta-Trypsin in Complex with Benzylamine, PDB code: 2bza:

Chlorine binding site 1 out of 1 in 2bza

Go back to Chlorine Binding Sites List in 2bza
Chlorine binding site 1 out of 1 in the Bovine Pancreas Beta-Trypsin in Complex with Benzylamine


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Bovine Pancreas Beta-Trypsin in Complex with Benzylamine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl2

b:46.1
occ:1.00
NE2 A:GLN240 3.7 30.4 1.0
CG A:GLN240 4.7 27.8 1.0
CD A:GLN240 4.7 31.8 1.0

Reference:

N.Ota, C.Stroupe, J.M.Ferreira-Da-Silva, S.A.Shah, M.Mares-Guia, A.T.Brunger. Non-Boltzmann Thermodynamic Integration (Nbti) For Macromolecular Systems: Relative Free Energy of Binding of Trypsin to Benzamidine and Benzylamine. Proteins V. 37 641 1999.
ISSN: ISSN 0887-3585
PubMed: 10651279
DOI: 10.1002/(SICI)1097-0134(19991201)37:4<641::AID-PROT14>3.0.CO;2-W
Page generated: Sat Jul 20 06:01:41 2024

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