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Potassium in PDB 8s1x: Crystal Structure of Actinonin-Bound PDF1 and the Computationally Designed DBACT553_1 Protein Binder

Enzymatic activity of Crystal Structure of Actinonin-Bound PDF1 and the Computationally Designed DBACT553_1 Protein Binder

All present enzymatic activity of Crystal Structure of Actinonin-Bound PDF1 and the Computationally Designed DBACT553_1 Protein Binder:
3.5.1.88;

Protein crystallography data

The structure of Crystal Structure of Actinonin-Bound PDF1 and the Computationally Designed DBACT553_1 Protein Binder, PDB code: 8s1x was solved by A.Marchand, M.Pacesa, B.E.Correia, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 55.70 / 1.88
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.44, 75.01, 83.16, 90, 90, 90
R / Rfree (%) 18.4 / 20.3

Other elements in 8s1x:

The structure of Crystal Structure of Actinonin-Bound PDF1 and the Computationally Designed DBACT553_1 Protein Binder also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of Actinonin-Bound PDF1 and the Computationally Designed DBACT553_1 Protein Binder (pdb code 8s1x). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Crystal Structure of Actinonin-Bound PDF1 and the Computationally Designed DBACT553_1 Protein Binder, PDB code: 8s1x:

Potassium binding site 1 out of 1 in 8s1x

Go back to Potassium Binding Sites List in 8s1x
Potassium binding site 1 out of 1 in the Crystal Structure of Actinonin-Bound PDF1 and the Computationally Designed DBACT553_1 Protein Binder


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 Actinonin-Bound PDF1 and the Computationally Designed DBACT553_1 Protein Binder within 5.0Å range:
probe atom residue distance (Å) B Occ
B:K101

b:89.0
occ:1.00
 HB2 B:HIS41 3.0 86.8 1.0
O A:HOH314 3.1 55.8 1.0
ND1 B:HIS41 3.2 103.5 1.0
O A:TYR99 3.3 41.0 1.0
H A:TYR99 3.3 48.1 1.0
CG B:HIS41 3.4 96.5 1.0
HB2 A:TYR99 3.5 55.1 1.0
CB B:HIS41 3.6 72.3 1.0
CE1 B:HIS41 3.8 106.5 1.0
HE21 A:GLN89 3.9 52.4 1.0
CD2 B:HIS41 4.0 104.6 1.0
HB3 B:PHE37 4.0 55.4 1.0
N A:TYR99 4.1 40.1 1.0
HD2 A:TYR99 4.1 51.2 1.0
O B:PHE37 4.1 55.5 1.0
HA B:HIS41 4.1 82.4 1.0
OE2 A:GLU100 4.2 56.5 1.0
HE1 B:HIS41 4.2 127.9 1.0
NE2 B:HIS41 4.2 111.2 1.0
HE22 A:GLN89 4.2 52.4 1.0
C A:TYR99 4.3 41.0 1.0
CB A:TYR99 4.4 45.9 1.0
HA A:PHE98 4.4 46.7 1.0
HB3 B:HIS41 4.4 86.8 1.0
NE2 A:GLN89 4.4 43.6 1.0
CA B:HIS41 4.4 68.7 1.0
CA A:TYR99 4.5 40.6 1.0
HD2 B:HIS41 4.6 125.6 1.0
H B:HIS41 4.7 73.2 1.0
N B:HIS41 4.8 61.0 1.0
C B:PHE37 4.9 50.8 1.0
HE2 B:HIS41 4.9 133.4 1.0
HA B:PHE37 4.9 55.2 1.0
CB B:PHE37 4.9 46.1 1.0
CD2 A:TYR99 5.0 42.7 1.0
CD A:GLU100 5.0 54.7 1.0
HG2 A:GLU100 5.0 47.3 1.0

Reference:

A.Marchand, S.Buckley, A.Schneuing, M.Pacesa, P.Gainza, E.Elizarova, R.Neeser, L.Reymond, S.Georgeon, J.Schmidt, B.E.Correia. Targeting Hybrid Neosurface Fingerprints For the Design of De Novo Drug-Induced Protein Interactions To Be Published.
Page generated: Wed Nov 13 11:16:45 2024

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