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Sodium in PDB 3rwk: First Crystal Structure of An Endo-Inulinase, From Aspergillus Ficuum: Structural Analysis and Comparison with Other GH32 Enzymes.

Enzymatic activity of First Crystal Structure of An Endo-Inulinase, From Aspergillus Ficuum: Structural Analysis and Comparison with Other GH32 Enzymes.

All present enzymatic activity of First Crystal Structure of An Endo-Inulinase, From Aspergillus Ficuum: Structural Analysis and Comparison with Other GH32 Enzymes.:
3.2.1.7;

Protein crystallography data

The structure of First Crystal Structure of An Endo-Inulinase, From Aspergillus Ficuum: Structural Analysis and Comparison with Other GH32 Enzymes., PDB code: 3rwk was solved by C.Michaux, J.Pouyez, G.Roussel, A.Mayard, A.M.Vandamme, I.Housen, J.Wouters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 9.99 / 2.10
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 95.760, 95.760, 130.820, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / 23.2

Sodium Binding Sites:

The binding sites of Sodium atom in the First Crystal Structure of An Endo-Inulinase, From Aspergillus Ficuum: Structural Analysis and Comparison with Other GH32 Enzymes. (pdb code 3rwk). 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 First Crystal Structure of An Endo-Inulinase, From Aspergillus Ficuum: Structural Analysis and Comparison with Other GH32 Enzymes., PDB code: 3rwk:

Sodium binding site 1 out of 1 in 3rwk

Go back to Sodium Binding Sites List in 3rwk
Sodium binding site 1 out of 1 in the First Crystal Structure of An Endo-Inulinase, From Aspergillus Ficuum: Structural Analysis and Comparison with Other GH32 Enzymes.


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of First Crystal Structure of An Endo-Inulinase, From Aspergillus Ficuum: Structural Analysis and Comparison with Other GH32 Enzymes. within 5.0Å range:
probe atom residue distance (Å) B Occ
X:Na521

b:12.4
occ:1.00
 O X:ARG295 2.2 25.2 1.0
O X:ASN265 2.4 27.6 1.0
OD1 X:ASP298 2.4 23.7 1.0
O X:HOH551 2.4 24.5 1.0
O X:HOH574 2.5 25.5 1.0
OD2 X:ASP298 2.6 22.9 1.0
O X:HOH557 2.6 25.8 1.0
OD1 X:ASN265 2.6 46.2 1.0
CG X:ASP298 2.8 23.3 1.0
C X:ASN265 3.3 27.8 1.0
C X:ARG295 3.4 22.8 1.0
CG X:ASN265 3.6 40.0 1.0
CA X:ASN265 4.0 29.6 1.0
N X:ASN265 4.1 28.3 1.0
O X:PHE297 4.1 24.1 1.0
CA X:ARG295 4.1 23.0 1.0
N X:GLY266 4.1 27.1 1.0
CB X:SER321 4.2 23.4 1.0
CA X:GLY266 4.3 26.9 1.0
CB X:ASP298 4.4 22.4 1.0
CB X:ASN265 4.4 29.4 1.0
N X:ASP296 4.4 22.3 1.0
O X:GLY294 4.5 26.1 1.0
ND2 X:ASN265 4.5 43.5 1.0
O3 X:MAN519 4.5 30.9 1.0
N X:PHE297 4.5 22.7 1.0
OG X:SER260 4.7 31.2 1.0
C X:GLY264 4.8 29.2 1.0
C X:PHE297 4.8 23.6 1.0
O X:GLY263 4.8 30.8 1.0
CA X:ASP296 4.8 23.3 1.0
O X:HOH537 4.9 23.7 1.0

Reference:

J.Pouyez, A.Mayard, A.M.Vandamme, G.Roussel, E.A.Perpete, J.Wouters, I.Housen, C.Michaux. First Crystal Structure of An Endo-Inulinase, INU2, From Aspergillus Ficuum: Discovery of An Extra-Pocket in the Catalytic Domain Responsible For Its Endo-Activity. Biochimie V. 94 2423 2012.
ISSN: ISSN 0300-9084
PubMed: 22750808
DOI: 10.1016/J.BIOCHI.2012.06.020
Page generated: Mon Oct 7 12:52:41 2024

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