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Sodium in PDB 2ghe: 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: 2ghe 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) 27.05 / 1.75
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 82.003, 82.003, 75.012, 90.00, 90.00, 90.00
R / Rfree (%) 18 / 22

Other elements in 2ghe:

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

Iron (Fe) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Conformational Mobility in the Active Site of A Heme Peroxidase (pdb code 2ghe). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Conformational Mobility in the Active Site of A Heme Peroxidase, PDB code: 2ghe:

Sodium binding site 1 out of 1 in 2ghe

Go back to Sodium Binding Sites List in 2ghe
Sodium 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 Sodium with other atoms in the Na 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:Na9252

b:46.4
occ:1.00
O X:ILE185 2.6 14.1 1.0
O X:THR164 2.8 15.5 1.0
O X:ASN182 2.9 19.0 1.0
OG1 X:THR180 3.0 19.2 1.0
OD1 X:ASP187 3.1 21.4 1.0
OG1 X:THR164 3.3 19.4 1.0
CB X:THR180 3.6 18.8 1.0
C X:ILE185 3.8 13.9 1.0
C X:ASN182 3.8 19.0 1.0
CG2 X:THR180 3.8 18.7 1.0
C X:THR164 3.9 15.6 1.0
CG X:ASP187 3.9 20.3 1.0
CB X:SER189 4.1 20.0 1.0
CB X:ASN182 4.1 20.9 1.0
O X:HOH9466 4.2 44.9 1.0
CB X:THR164 4.3 15.0 1.0
N X:ASP187 4.3 14.7 1.0
CB X:ILE185 4.3 13.8 1.0
CA X:ASN182 4.4 19.8 1.0
CA X:THR164 4.4 14.9 1.0
OD2 X:ASP187 4.4 25.5 1.0
CA X:ILE185 4.5 14.0 1.0
OG X:SER189 4.5 23.4 1.0
N X:ASN182 4.6 19.2 1.0
N X:ILE185 4.7 13.9 1.0
CG2 X:THR164 4.7 12.5 1.0
N X:PHE186 4.8 13.7 1.0
N X:PRO183 4.8 18.8 1.0
CG2 X:ILE185 4.8 15.2 1.0
CA X:PHE186 4.9 13.3 1.0
N X:ILE165 5.0 15.4 1.0
C X:PHE186 5.0 13.9 1.0
CA X:PRO183 5.0 17.9 1.0
CB X:ASP187 5.0 16.9 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: Tue Dec 15 05:49:47 2020

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