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Sodium in PDB 2whm: Cellvibrio Japonicus MAN26A E121A and E320G Double Mutant in Complex with Mannobiose

Enzymatic activity of Cellvibrio Japonicus MAN26A E121A and E320G Double Mutant in Complex with Mannobiose

All present enzymatic activity of Cellvibrio Japonicus MAN26A E121A and E320G Double Mutant in Complex with Mannobiose:
3.2.1.78;

Protein crystallography data

The structure of Cellvibrio Japonicus MAN26A E121A and E320G Double Mutant in Complex with Mannobiose, PDB code: 2whm was solved by V.M.A.Ducros, G.J.Davies, J.E.Flint, H.J.Gilbert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.98 / 1.50
Space group P 41
Cell size a, b, c (Å), α, β, γ (°) 93.177, 93.177, 53.780, 90.00, 90.00, 90.00
R / Rfree (%) 14.4 / 16.5

Other elements in 2whm:

The structure of Cellvibrio Japonicus MAN26A E121A and E320G Double Mutant in Complex with Mannobiose also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Cellvibrio Japonicus MAN26A E121A and E320G Double Mutant in Complex with Mannobiose (pdb code 2whm). 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 Cellvibrio Japonicus MAN26A E121A and E320G Double Mutant in Complex with Mannobiose, PDB code: 2whm:

Sodium binding site 1 out of 1 in 2whm

Go back to Sodium Binding Sites List in 2whm
Sodium binding site 1 out of 1 in the Cellvibrio Japonicus MAN26A E121A and E320G Double Mutant in Complex with Mannobiose


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Cellvibrio Japonicus MAN26A E121A and E320G Double Mutant in Complex with Mannobiose within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1425

b:12.7
occ:1.00
 O A:ARG69 2.2 13.0 1.0
O A:ARG352 2.2 13.5 1.0
O A:ILE354 2.3 10.9 1.0
O A:SER72 2.3 13.3 1.0
C A:ARG69 3.3 12.9 1.0
CG1 A:ILE73 3.3 12.9 1.0
C A:SER72 3.3 12.7 1.0
C A:ARG352 3.4 13.0 1.0
C A:ILE354 3.4 11.3 1.0
C A:GLU353 3.5 12.0 1.0
N A:ILE354 3.6 11.9 1.0
CA A:GLU353 3.7 12.0 1.0
CA A:ARG69 3.8 12.8 1.0
N A:GLU353 3.9 12.9 1.0
N A:ILE73 4.0 12.4 1.0
CE2 A:PHE404 4.0 14.8 1.0
CA A:ILE73 4.0 12.1 1.0
O A:GLU353 4.0 12.3 1.0
CZ A:PHE404 4.0 14.9 1.0
CA A:ILE354 4.1 11.6 1.0
CB A:ILE73 4.3 11.9 1.0
N A:SER72 4.3 13.6 1.0
CB A:ARG69 4.3 12.7 1.0
CD1 A:ILE73 4.3 13.6 1.0
CA A:SER72 4.4 13.3 1.0
N A:ARG70 4.4 13.5 1.0
N A:ALA355 4.4 10.6 1.0
CG1 A:ILE354 4.6 12.2 1.0
CA A:ARG352 4.6 13.0 1.0
CA A:ALA355 4.6 11.1 1.0
CA A:ARG70 4.8 13.6 1.0
NE2 A:GLN68 4.9 13.3 1.0
O A:GLN68 4.9 13.1 1.0
N A:HIS71 4.9 13.4 1.0

Reference:

L.E.Tailford, V.M.A.Ducros, J.E.Flint, S.M.Roberts, C.Morland, D.L.Zechel, N.Smith, M.E.Bjornvad, T.V.Borchert, K.S.Wilson, G.J.Davies, H.J.Gilbert. Understanding How Diverse -Mannanases Recognise Heterogeneous Substrates. Biochemistry V. 48 7009 2009.
ISSN: ISSN 0006-2960
PubMed: 19441796
DOI: 10.1021/BI900515D
Page generated: Mon Oct 7 04:40:25 2024

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