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Sodium in PDB 6aw4: 1.50A Resolution Structure of Catechol O-Methyltransferase (Comt) From Nannospalax Galili

Protein crystallography data

The structure of 1.50A Resolution Structure of Catechol O-Methyltransferase (Comt) From Nannospalax Galili, PDB code: 6aw4 was solved by S.Lovell, N.Mehzabeen, K.P.Battaile, Y.Deng, R.P.Hanzlik, I.Shams, J.Moskovitz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.46 / 1.50
Space group P 62
Cell size a, b, c (Å), α, β, γ (°) 94.755, 94.755, 75.934, 90.00, 90.00, 120.00
R / Rfree (%) 15.4 / 17

Sodium Binding Sites:

The binding sites of Sodium atom in the 1.50A Resolution Structure of Catechol O-Methyltransferase (Comt) From Nannospalax Galili (pdb code 6aw4). 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 1.50A Resolution Structure of Catechol O-Methyltransferase (Comt) From Nannospalax Galili, PDB code: 6aw4:

Sodium binding site 1 out of 1 in 6aw4

Go back to Sodium Binding Sites List in 6aw4
Sodium binding site 1 out of 1 in the 1.50A Resolution Structure of Catechol O-Methyltransferase (Comt) From Nannospalax Galili


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of 1.50A Resolution Structure of Catechol O-Methyltransferase (Comt) From Nannospalax Galili within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na303

b:16.1
occ:1.00
O A:SER185 2.3 16.9 1.0
O A:VAL182 2.4 15.4 1.0
O A:PHE188 2.4 16.7 1.0
O A:ARG183 2.5 17.1 1.0
C A:ARG183 3.1 16.3 1.0
CA A:ARG183 3.4 16.8 1.0
C A:SER185 3.4 16.7 1.0
C A:VAL182 3.5 14.1 1.0
C A:PHE188 3.5 15.3 1.0
N A:SER185 3.9 16.5 1.0
N A:ARG183 4.0 15.6 1.0
N A:PHE188 4.1 15.9 1.0
N A:GLY184 4.1 15.6 1.0
CA A:PHE188 4.1 15.3 1.0
CB A:PHE188 4.2 15.2 1.0
CA A:SER185 4.2 16.8 1.0
C A:GLY184 4.2 16.9 1.0
SG A:CYS190 4.3 17.2 1.0
N A:SER186 4.4 16.6 1.0
CA A:SER186 4.6 17.5 0.5
CA A:SER186 4.6 17.5 0.5
N A:GLU189 4.6 15.3 1.0
O A:GLY184 4.7 18.1 1.0
CA A:GLY184 4.7 16.9 1.0
CB A:ARG183 4.7 16.9 1.0
CB A:SER185 4.8 18.1 1.0
CA A:VAL182 4.8 14.8 1.0
C A:SER186 4.9 18.4 1.0
CA A:GLU189 5.0 16.1 1.0

Reference:

Y.Deng, S.Lovell, N.Mehzabeen, K.P.Battaile, R.P.Hanzlik, I.Shams, J.Moskovitz. Crystal Structure of the Catechol-O-Methyl Transferase (Comt) Enzyme of the Subterranean Mole Rat (Spalax) and the Effect of L136M Substitution To Be Published.
Page generated: Mon Aug 18 03:40:18 2025

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