Potassium in PDB 9arc: Crystal Structure of C0362 (TDE_0362 [TDE0362] Resi 205-647)

Protein crystallography data

The structure of Crystal Structure of C0362 (TDE_0362 [TDE0362] Resi 205-647), PDB code: 9arc was solved by N.D.Clark, M.G.Malkowski, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.35 / 1.77
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 41.598, 99.258, 121.31, 90, 90, 90
R / Rfree (%) 19.8 / 22.7

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of C0362 (TDE_0362 [TDE0362] Resi 205-647) (pdb code 9arc). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Crystal Structure of C0362 (TDE_0362 [TDE0362] Resi 205-647), PDB code: 9arc:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in 9arc

Go back to Potassium Binding Sites List in 9arc
Potassium binding site 1 out of 3 in the Crystal Structure of C0362 (TDE_0362 [TDE0362] Resi 205-647)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of C0362 (TDE_0362 [TDE0362] Resi 205-647) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K701

b:53.3
occ:1.00
O A:HOH856 3.0 60.5 1.0
O A:HOH863 3.1 43.4 1.0
CG A:PRO256 3.7 52.3 1.0
CB A:PRO256 3.7 49.7 1.0
CE1 A:TYR603 4.0 50.5 1.0
N A:TRP257 4.0 40.6 1.0
C A:PRO256 4.0 43.1 1.0
CB A:TRP257 4.1 38.0 1.0
CA A:TRP257 4.2 39.6 1.0
CD1 A:TYR603 4.3 52.4 1.0
O A:PRO256 4.3 47.5 1.0
CD1 A:LEU280 4.4 44.1 1.0
CA A:PRO256 4.5 44.0 1.0
NH1 A:ARG288 4.7 37.4 1.0
CG A:TRP257 5.0 37.9 1.0
CD1 A:TRP257 5.0 38.1 1.0

Potassium binding site 2 out of 3 in 9arc

Go back to Potassium Binding Sites List in 9arc
Potassium binding site 2 out of 3 in the Crystal Structure of C0362 (TDE_0362 [TDE0362] Resi 205-647)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of C0362 (TDE_0362 [TDE0362] Resi 205-647) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K702

b:53.1
occ:1.00
N A:PHE250 3.4 45.4 1.0
CB A:ALA261 3.5 47.5 1.0
CA A:ALA261 3.7 49.5 1.0
CD A:PRO262 4.0 47.1 1.0
CA A:TYR249 4.1 45.5 1.0
CB A:PHE250 4.1 46.7 1.0
C A:TYR249 4.2 39.0 1.0
CD2 A:PHE250 4.3 39.9 1.0
CA A:PHE250 4.3 45.1 1.0
CD1 A:TYR249 4.3 63.8 1.0
O A:PHE250 4.4 50.0 1.0
N A:ALA261 4.5 46.2 1.0
CB A:TYR249 4.6 46.4 1.0
CG A:PHE250 4.7 41.4 1.0
CB A:SER253 4.7 70.4 1.0
C A:ALA261 4.8 46.9 1.0
C A:PHE250 4.8 47.0 1.0
N A:PRO262 4.8 44.4 1.0
O A:GLY260 4.9 50.6 1.0
CA A:SER253 4.9 62.8 1.0
CG A:TYR249 5.0 54.1 1.0
C A:GLY260 5.0 49.6 1.0

Potassium binding site 3 out of 3 in 9arc

Go back to Potassium Binding Sites List in 9arc
Potassium binding site 3 out of 3 in the Crystal Structure of C0362 (TDE_0362 [TDE0362] Resi 205-647)


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Crystal Structure of C0362 (TDE_0362 [TDE0362] Resi 205-647) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K703

b:38.9
occ:1.00
O A:HOH1024 2.6 47.9 1.0
O A:HOH874 3.1 35.9 1.0
O A:HOH920 3.2 45.0 1.0
CD2 A:TYR603 3.5 51.8 1.0
CB A:ARG288 3.6 33.9 1.0
CE2 A:TYR603 3.7 49.9 1.0
CA A:ARG288 3.8 31.9 1.0
N A:ARG289 3.9 35.1 1.0
N A:ILE602 3.9 57.4 1.0
OD1 A:ASN601 4.0 69.2 1.0
CG A:ASN601 4.0 61.1 1.0
ND2 A:ASN601 4.1 64.1 1.0
CA A:ASN601 4.2 59.4 1.0
CG1 A:ILE602 4.2 50.8 1.0
O A:HOH818 4.4 43.5 1.0
C A:ARG288 4.4 34.2 1.0
O A:ASN287 4.5 32.2 1.0
C A:ASN601 4.6 65.9 1.0
CB A:ASN601 4.7 67.3 1.0
CG A:TYR603 4.8 53.1 1.0
CA A:ILE602 4.9 62.0 1.0
O A:GLY600 4.9 59.1 1.0
O A:ARG289 4.9 37.9 1.0
N A:TYR603 4.9 54.4 1.0
N A:ARG288 5.0 34.6 1.0
O A:HOH859 5.0 31.5 1.0
CB A:ILE602 5.0 56.7 1.0

Reference:

K.Kurniyati, N.D.Clark, H.Wang, Y.Deng, C.W.Sze, M.B.Visser, J.P.Balthasar, M.G.Malkowski, C.Li. A Dual Domain Bacterial Virulence Factor Annihilates Host Innate Immune Defenses Via Degrading Complement Factors and Blocking Neutrophils Chemotaxis To Be Published.
Page generated: Tue Dec 10 20:24:03 2024

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