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Chlorine in PDB 1bju: Beta-Trypsin Complexed with Acpu

Enzymatic activity of Beta-Trypsin Complexed with Acpu

All present enzymatic activity of Beta-Trypsin Complexed with Acpu:
3.4.21.4;

Protein crystallography data

The structure of Beta-Trypsin Complexed with Acpu, PDB code: 1bju was solved by S.Presnell, G.Patil, C.Mura, K.Jude, J.Conley, C.Kam, J.Bertrand, J.Powers, L.Williams, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 7.00 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 54.840, 58.490, 67.830, 90.00, 90.00, 90.00
R / Rfree (%) 17.1 / n/a

Other elements in 1bju:

The structure of Beta-Trypsin Complexed with Acpu also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Beta-Trypsin Complexed with Acpu (pdb code 1bju). 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 Beta-Trypsin Complexed with Acpu, PDB code: 1bju:

Chlorine binding site 1 out of 1 in 1bju

Go back to Chlorine Binding Sites List in 1bju
Chlorine binding site 1 out of 1 in the Beta-Trypsin Complexed with Acpu


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Beta-Trypsin Complexed with Acpu within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl910

b:30.6
occ:1.00
CL A:GP6910 0.0 30.6 1.0
C12 A:GP6910 1.7 27.2 1.0
C13 A:GP6910 2.7 28.4 1.0
C11 A:GP6910 2.7 25.5 1.0
O A:HOH666 3.2 29.9 1.0
O A:HOH686 3.9 41.8 1.0
C14 A:GP6910 4.0 27.2 1.0
O A:HOH532 4.0 14.4 1.0
C10 A:GP6910 4.0 24.8 1.0
CB A:HIS57 4.3 7.5 1.0
CD2 A:LEU99 4.4 10.6 1.0
O A:SER96 4.4 12.4 1.0
OH A:TYR94 4.4 5.9 1.0
C9 A:GP6910 4.5 24.9 1.0
CG A:HIS57 4.9 8.6 1.0

Reference:

S.R.Presnell, G.S.Patil, C.Mura, K.M.Jude, J.M.Conley, J.A.Bertrand, C.M.Kam, J.C.Powers, L.D.Williams. Oxyanion-Mediated Inhibition of Serine Proteases. Biochemistry V. 37 17068 1998.
ISSN: ISSN 0006-2960
PubMed: 9836602
DOI: 10.1021/BI981636U
Page generated: Sat Dec 12 08:31:56 2020

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