Chlorine in PDB 4jk6: Human Urokinase-Type Plasminogen Activator (Upa) in Complex with A Bicyclic Peptide Inhibitor (UK18-D-Aba)

Enzymatic activity of Human Urokinase-Type Plasminogen Activator (Upa) in Complex with A Bicyclic Peptide Inhibitor (UK18-D-Aba)

All present enzymatic activity of Human Urokinase-Type Plasminogen Activator (Upa) in Complex with A Bicyclic Peptide Inhibitor (UK18-D-Aba):
3.4.21.73;

Protein crystallography data

The structure of Human Urokinase-Type Plasminogen Activator (Upa) in Complex with A Bicyclic Peptide Inhibitor (UK18-D-Aba), PDB code: 4jk6 was solved by S.A.Buth, P.G.Leiman, S.Chen, C.Heinis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 33.16 / 2.20
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 121.219, 121.219, 42.731, 90.00, 90.00, 120.00
R / Rfree (%) 15.3 / 20.5

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Human Urokinase-Type Plasminogen Activator (Upa) in Complex with A Bicyclic Peptide Inhibitor (UK18-D-Aba) (pdb code 4jk6). 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 Human Urokinase-Type Plasminogen Activator (Upa) in Complex with A Bicyclic Peptide Inhibitor (UK18-D-Aba), PDB code: 4jk6:

Chlorine binding site 1 out of 1 in 4jk6

Go back to Chlorine Binding Sites List in 4jk6
Chlorine binding site 1 out of 1 in the Human Urokinase-Type Plasminogen Activator (Upa) in Complex with A Bicyclic Peptide Inhibitor (UK18-D-Aba)


Mono view


Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Human Urokinase-Type Plasminogen Activator (Upa) in Complex with A Bicyclic Peptide Inhibitor (UK18-D-Aba) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cl305

b:68.7
occ:1.00
 N A:LYS92 2.9 46.3 1.0
NE1 A:TRP237 3.2 36.8 1.0
CG A:LYS92 3.4 54.6 1.0
CB A:LYS92 3.4 53.5 1.0
O A:LEU90 3.5 38.1 1.0
CA A:HIS91 3.7 38.9 1.0
C A:HIS91 3.8 42.2 1.0
CA A:LYS92 3.8 49.0 1.0
CE2 A:TRP237 4.0 34.5 1.0
NE2 A:HIS241 4.0 64.8 1.0
CD A:LYS92 4.1 59.6 1.0
CE1 A:HIS241 4.2 62.1 1.0
CZ2 A:TRP237 4.2 33.0 1.0
CD1 A:TRP237 4.2 38.0 1.0
ND1 A:HIS91 4.3 43.2 1.0
CG A:HIS91 4.3 40.0 1.0
C A:LEU90 4.4 35.4 1.0
N A:HIS91 4.5 35.8 1.0
CE1 A:HIS91 4.6 44.7 1.0
CB A:HIS91 4.6 37.7 1.0
CD2 A:HIS91 4.6 40.1 1.0
NE2 A:HIS91 4.8 42.9 1.0
O A:HOH406 4.8 50.9 1.0
C A:LYS92 4.9 49.4 1.0
N A:ASP93 4.9 49.5 1.0
O A:HIS91 5.0 42.6 1.0

Reference:

S.Chen, D.Gfeller, S.A.Buth, O.Michielin, P.G.Leiman, C.Heinis. Improving Binding Affinity and Stability of Peptide Ligands By Substituting Glycines with D-Amino Acids. Chembiochem V. 14 1316 2013.
ISSN: ISSN 1439-4227
PubMed: 23828687
DOI: 10.1002/CBIC.201300228
Page generated: Sat Dec 12 10:48:18 2020

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