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Bromine in PDB 2yj2: Cathepsin L with A Nitrile Inhibitor

Enzymatic activity of Cathepsin L with A Nitrile Inhibitor

All present enzymatic activity of Cathepsin L with A Nitrile Inhibitor:
3.4.22.15;

Protein crystallography data

The structure of Cathepsin L with A Nitrile Inhibitor, PDB code: 2yj2 was solved by D.W.Banner, J.M.Benz, W.Haap, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.59 / 1.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 45.883, 57.147, 75.599, 90.00, 90.00, 90.00
R / Rfree (%) 14.535 / 17.855

Other elements in 2yj2:

The structure of Cathepsin L with A Nitrile Inhibitor also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Bromine Binding Sites:

The binding sites of Bromine atom in the Cathepsin L with A Nitrile Inhibitor (pdb code 2yj2). This binding sites where shown within 5.0 Angstroms radius around Bromine atom.
In total only one binding site of Bromine was determined in the Cathepsin L with A Nitrile Inhibitor, PDB code: 2yj2:

Bromine binding site 1 out of 1 in 2yj2

Go back to Bromine Binding Sites List in 2yj2
Bromine binding site 1 out of 1 in the Cathepsin L with A Nitrile Inhibitor


Mono view


Stereo pair view

A full contact list of Bromine with other atoms in the Br binding site number 1 of Cathepsin L with A Nitrile Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Br1221

b:18.2
occ:1.00
BR3 A:YJ21221 0.0 18.2 1.0
C27 A:YJ21221 1.9 14.8 1.0
C26 A:YJ21221 2.9 16.7 1.0
C28 A:YJ21221 2.9 14.8 1.0
HA2 A:GLY68 2.9 10.4 1.0
H37 A:YJ21221 3.0 15.7 1.0
H38 A:YJ21221 3.0 15.9 1.0
O A:GLY61 3.1 12.9 1.0
HE2 A:TYR72 3.3 12.8 1.0
HG3 A:GLU63 3.3 16.1 1.0
HA A:ASN62 3.5 11.3 1.0
O A:HOH2172 3.7 31.0 1.0
CD A:GLU63 3.8 23.8 1.0
CA A:GLY68 3.9 9.6 1.0
HG A:LEU69 3.9 13.5 1.0
HD2 A:TYR72 4.0 11.6 1.0
OE2 A:GLU63 4.0 30.6 1.0
CG A:GLU63 4.0 16.5 1.0
CE2 A:TYR72 4.1 13.1 1.0
OE1 A:GLU63 4.1 30.3 1.0
C25 A:YJ21221 4.2 14.9 1.0
C A:GLY61 4.2 11.3 1.0
C29 A:YJ21221 4.2 14.1 1.0
HB2 A:GLU63 4.2 14.7 1.0
N A:GLY68 4.3 10.6 1.0
H A:GLU63 4.3 11.6 1.0
CA A:ASN62 4.4 11.1 1.0
CD2 A:TYR72 4.4 12.3 1.0
C A:GLY68 4.5 8.8 1.0
O A:GLY67 4.5 12.2 1.0
HA3 A:GLY68 4.5 10.1 1.0
C A:GLY67 4.6 11.1 1.0
N A:GLU63 4.6 12.0 1.0
H A:LEU69 4.6 9.7 1.0
CB A:GLU63 4.7 13.7 1.0
OD1 A:ASN62 4.7 10.5 1.0
H A:GLY68 4.7 10.9 1.0
N A:LEU69 4.7 9.6 1.0
C24 A:YJ21221 4.7 14.0 1.0
N A:ASN62 4.8 11.3 1.0
C A:ASN62 4.8 11.1 1.0
HG2 A:GLU63 4.8 17.1 1.0
CG A:LEU69 4.9 11.3 1.0

Reference:

L.A.Hardegger, B.Kuhn, B.Spinnler, L.Anselm, R.Ecabert, M.Stihle, B.Gsell, R.Thoma, J.Diez, J.M.Benz, J.Plancher, G.Hartmann, Y.Isshiki, K.Morikami, N.Shimma, W.Haap, D.W.Banner, F.Diederich. Halogen Bonding at the Active Sites of Human Cathepsin L and MEK1 Kinase: Efficient Interactions in Different Environments. Chemmedchem V. 6 2048 2011.
ISSN: ISSN 1860-7179
PubMed: 21898833
DOI: 10.1002/CMDC.201100353
Page generated: Wed Jul 10 19:02:21 2024

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