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Potassium in PDB 2ghh: Conformational Mobility in the Active Site of A Heme Peroxidase

Enzymatic activity of Conformational Mobility in the Active Site of A Heme Peroxidase

All present enzymatic activity of Conformational Mobility in the Active Site of A Heme Peroxidase:
1.11.1.11;

Protein crystallography data

The structure of Conformational Mobility in the Active Site of A Heme Peroxidase, PDB code: 2ghh was solved by S.K.Badyal, M.G.Joyce, K.H.Sharp, E.L.Raven, P.C.E.Moody, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 18.86 / 2.01
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 82.692, 82.692, 74.772, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 25.8

Other elements in 2ghh:

The structure of Conformational Mobility in the Active Site of A Heme Peroxidase also contains other interesting chemical elements:

Iron (Fe) 1 atom

Potassium Binding Sites:

The binding sites of Potassium atom in the Conformational Mobility in the Active Site of A Heme Peroxidase (pdb code 2ghh). 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 Conformational Mobility in the Active Site of A Heme Peroxidase, PDB code: 2ghh:

Potassium binding site 1 out of 1 in 2ghh

Go back to Potassium Binding Sites List in 2ghh
Potassium binding site 1 out of 1 in the Conformational Mobility in the Active Site of A Heme Peroxidase


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Conformational Mobility in the Active Site of A Heme Peroxidase within 5.0Å range:
probe atom residue distance (Å) B Occ
X:K9252

b:43.7
occ:1.00
O X:THR164 2.4 18.6 1.0
O X:ILE185 2.4 15.6 1.0
O X:ASN182 2.6 20.2 1.0
ND2 X:ASN182 2.6 21.3 0.5
OG1 X:THR180 2.7 19.1 1.0
OG1 X:THR164 3.5 21.8 1.0
CB X:THR180 3.5 18.5 1.0
C X:ASN182 3.5 20.8 1.0
C X:THR164 3.5 17.8 1.0
CG X:ASN182 3.5 21.7 0.5
C X:ILE185 3.6 15.2 1.0
OD1 X:ASP187 3.7 23.0 1.0
CG2 X:THR180 3.8 18.2 1.0
CA X:THR164 4.2 18.1 1.0
OD1 X:ASN182 4.2 23.2 0.5
CB X:THR164 4.3 18.5 1.0
N X:ILE185 4.3 16.3 1.0
CA X:ASN182 4.3 21.1 0.5
CA X:ASN182 4.3 21.0 0.5
CA X:ILE185 4.3 15.6 1.0
CB X:ASN182 4.3 21.4 0.5
CB X:ASN182 4.3 21.7 0.5
N X:PRO183 4.4 20.1 1.0
CA X:PRO183 4.4 19.2 1.0
CB X:ILE185 4.4 14.9 1.0
N X:ASN182 4.5 21.2 1.0
CG X:ASP187 4.5 23.1 1.0
N X:ILE165 4.5 16.8 1.0
CB X:SER189 4.6 21.3 1.0
N X:ASP187 4.6 17.0 1.0
CG2 X:THR164 4.6 16.9 1.0
N X:PHE186 4.7 14.5 1.0
C X:PRO183 4.7 19.1 1.0
CA X:ILE165 4.8 16.0 1.0
CG2 X:ILE165 4.8 15.9 1.0
CA X:PHE186 4.9 15.2 1.0
OD2 X:ASP187 4.9 26.1 1.0
CG2 X:ILE185 4.9 15.0 1.0
CA X:THR180 5.0 18.6 1.0
OG X:SER189 5.0 23.9 1.0
O X:HOH9281 5.0 17.6 1.0

Reference:

S.K.Badyal, M.G.Joyce, K.H.Sharp, H.E.Seward, M.Mewies, J.Basran, I.K.Macdonald, P.C.E.Moody, E.L.Raven. Conformational Mobility in the Active Site of A Heme Peroxidase. J.Biol.Chem. V. 281 24512 2006.
ISSN: ISSN 0021-9258
PubMed: 16762924
DOI: 10.1074/JBC.M602602200
Page generated: Sun Dec 13 23:09:57 2020

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