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Sodium in PDB 1o8u: The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily

Protein crystallography data

The structure of The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily, PDB code: 1o8u was solved by G.Grogan, J.L.Whittingham, J.P.Turkenburg, C.S.Verma, M.A.Walsh, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 78.950, 130.410, 81.320, 90.00, 114.16, 90.00
R / Rfree (%) 14.7 / 19

Sodium Binding Sites:

The binding sites of Sodium atom in the The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily (pdb code 1o8u). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily, PDB code: 1o8u:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in 1o8u

Go back to Sodium Binding Sites List in 1o8u
Sodium binding site 1 out of 2 in the The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1253

b:16.8
occ:1.00
O A:HOH2131 2.4 12.9 1.0
O B:HOH2126 2.4 11.3 1.0
O A:HOH2130 2.4 14.0 1.0
O C:HOH2122 2.4 13.9 1.0
O B:HOH2123 2.4 14.0 1.0
O C:HOH2120 2.5 12.7 1.0
O B:ASP186 3.7 15.1 1.0
O C:ASP186 3.7 14.0 1.0
O A:ASP186 3.7 14.6 1.0
NH1 A:ARG168 4.0 14.1 1.0
NH1 B:ARG168 4.0 16.1 1.0
NH1 C:ARG168 4.0 18.7 1.0
O B:HOH2127 4.3 17.1 1.0
O B:HOH2102 4.3 17.1 1.0
O C:HOH2105 4.3 20.5 1.0
OD1 B:ASP186 4.4 18.0 1.0
O C:HOH2121 4.5 16.9 1.0
OD1 C:ASP186 4.5 15.1 1.0
OD1 A:ASP186 4.5 16.1 1.0
OD2 B:ASP186 4.7 16.1 1.0
OD2 A:ASP186 4.7 19.4 1.0
OD2 C:ASP186 4.8 19.5 1.0
NH2 B:ARG168 4.8 15.4 1.0
NH2 A:ARG168 4.8 13.3 1.0
C B:ASP186 4.8 14.5 1.0
C A:ASP186 4.8 14.9 1.0
C C:ASP186 4.8 14.7 1.0
CG B:ASP186 4.8 16.8 1.0
CZ B:ARG168 4.9 13.4 1.0
CZ A:ARG168 4.9 13.8 1.0
CG A:ASP186 4.9 15.9 1.0
CG C:ASP186 4.9 16.8 1.0
CZ C:ARG168 5.0 15.2 1.0

Sodium binding site 2 out of 2 in 1o8u

Go back to Sodium Binding Sites List in 1o8u
Sodium binding site 2 out of 2 in the The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of The 2 Angstrom Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Na1253

b:15.8
occ:1.00
O E:HOH2130 2.3 16.4 1.0
O F:HOH2116 2.3 13.6 1.0
O D:HOH2109 2.4 14.1 1.0
O E:HOH2129 2.4 15.2 1.0
O F:HOH2113 2.5 16.0 1.0
O F:HOH2115 2.5 16.3 1.0
O E:ASP186 3.7 16.7 1.0
O D:ASP186 3.7 18.2 1.0
O F:ASP186 3.8 17.1 1.0
NH1 E:ARG168 4.0 16.2 1.0
NH1 F:ARG168 4.0 17.6 1.0
NH1 D:ARG168 4.1 17.1 1.0
O E:HOH2111 4.3 18.6 1.0
O F:HOH2118 4.4 15.0 1.0
O D:HOH2108 4.4 24.3 1.0
O F:HOH2101 4.4 18.4 1.0
OD2 D:ASP186 4.5 17.2 1.0
OD1 F:ASP186 4.5 15.6 1.0
OD1 E:ASP186 4.5 17.4 1.0
OD2 E:ASP186 4.7 16.8 1.0
OD1 D:ASP186 4.7 16.4 1.0
OD2 F:ASP186 4.7 18.6 1.0
NH2 F:ARG168 4.8 18.2 1.0
NH2 E:ARG168 4.8 18.5 1.0
C E:ASP186 4.8 16.5 1.0
CZ E:ARG168 4.9 15.3 1.0
CZ F:ARG168 4.9 16.4 1.0
CG E:ASP186 4.9 18.3 1.0
CG D:ASP186 4.9 16.2 1.0
C F:ASP186 4.9 16.7 1.0
C D:ASP186 4.9 16.9 1.0
NH2 D:ARG168 4.9 16.6 1.0
CG F:ASP186 4.9 16.2 1.0
CZ D:ARG168 5.0 17.8 1.0

Reference:

J.L.Whittingham, J.P.Turkenburg, C.S.Verma, M.A.Walsh, G.Grogan. The 2 A Crystal Structure of 6-Oxo Camphor Hydrolase: New Structural Diversity in the Crotonase Superfamily J.Biol.Chem. V. 278 1744 2003.
ISSN: ISSN 0021-9258
PubMed: 12421807
DOI: 10.1074/JBC.M211188200
Page generated: Sun Aug 17 06:50:57 2025

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