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Sodium in PDB 1ej2: Crystal Structure of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase with Bound Nad+

Enzymatic activity of Crystal Structure of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase with Bound Nad+

All present enzymatic activity of Crystal Structure of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase with Bound Nad+:
2.7.7.1;

Protein crystallography data

The structure of Crystal Structure of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase with Bound Nad+, PDB code: 1ej2 was solved by V.Saridakis, D.Christendat, M.S.Kimber, A.M.Edwards, E.F.Pai, Midwestcenter For Structural Genomics (Mcsg), Northeast Structural Genomicsconsortium (Nesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.30 / 1.90
Space group P 63 2 2
Cell size a, b, c (Å), α, β, γ (°) 89.084, 89.084, 109.926, 90.00, 90.00, 120.00
R / Rfree (%) 21.1 / 24.1

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase with Bound Nad+ (pdb code 1ej2). 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 Crystal Structure of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase with Bound Nad+, PDB code: 1ej2:

Sodium binding site 1 out of 1 in 1ej2

Go back to Sodium Binding Sites List in 1ej2
Sodium binding site 1 out of 1 in the Crystal Structure of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase with Bound Nad+


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Methanobacterium Thermoautotrophicum Nicotinamide Mononucleotide Adenylyltransferase with Bound Nad+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na1000

b:39.6
occ:1.00
 O3 A:SO41759 2.6 37.2 1.0
N A:GLN13 3.0 27.1 1.0
O1A A:NAD1339 3.1 36.3 1.0
O2A A:NAD1339 3.5 37.6 1.0
N A:MET12 3.6 27.4 1.0
NH1 A:ARG11 3.7 32.5 1.0
PA A:NAD1339 3.7 37.0 1.0
CA A:GLN13 3.8 27.0 1.0
CB A:GLN13 3.8 27.2 1.0
S A:SO41759 3.8 36.6 1.0
O2 A:SO41759 3.8 37.1 1.0
C A:MET12 4.0 26.5 1.0
CA A:MET12 4.0 27.4 1.0
CB A:ARG11 4.0 29.2 1.0
CZ A:ARG11 4.0 32.1 1.0
NH2 A:ARG11 4.1 31.4 1.0
C A:GLN13 4.1 27.3 1.0
O A:GLN13 4.2 27.1 1.0
C A:ARG11 4.2 27.2 1.0
CA A:GLY132 4.2 36.2 1.0
NH1 A:ARG136 4.4 27.1 1.0
CE1 A:HIS19 4.4 32.6 1.0
O3 A:NAD1339 4.4 38.5 1.0
CA A:ARG11 4.5 28.6 1.0
N A:GLY132 4.6 37.4 1.0
NE2 A:HIS19 4.6 33.7 1.0
CG A:GLN13 4.6 26.4 1.0
N A:ARG11 4.7 28.8 1.0
O1 A:SO41759 4.7 35.8 1.0
O A:PRO14 4.8 27.9 1.0
O4 A:SO41759 4.8 36.4 1.0
CG A:ARG11 4.9 29.9 1.0
NE A:ARG11 4.9 32.4 1.0
O A:ARG11 5.0 27.1 1.0

Reference:

V.Saridakis, D.Christendat, M.S.Kimber, A.Dharamsi, A.M.Edwards, E.F.Pai. Insights Into Ligand Binding and Catalysis of A Central Step in Nad+ Synthesis: Structures of Methanobacterium Thermoautotrophicum Nmn Adenylyltransferase Complexes. J.Biol.Chem. V. 276 7225 2001.
ISSN: ISSN 0021-9258
PubMed: 11063748
DOI: 10.1074/JBC.M008810200
Page generated: Sun Oct 6 18:22:30 2024

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