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Sodium in PDB 1w6g: Agao Holoenzyme at 1.55 Angstroms

Enzymatic activity of Agao Holoenzyme at 1.55 Angstroms

All present enzymatic activity of Agao Holoenzyme at 1.55 Angstroms:
1.4.3.6;

Protein crystallography data

The structure of Agao Holoenzyme at 1.55 Angstroms, PDB code: 1w6g was solved by D.B.Langley, A.P.Duff, G.A.Juda, E.M.Shepard, D.M.Dooley, H.C.Freeman, J.M.Guss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.82 / 1.55
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 157.836, 63.243, 91.982, 90.00, 112.03, 90.00
R / Rfree (%) 17 / 18.8

Other elements in 1w6g:

The structure of Agao Holoenzyme at 1.55 Angstroms also contains other interesting chemical elements:

Copper (Cu) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Agao Holoenzyme at 1.55 Angstroms (pdb code 1w6g). 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 Agao Holoenzyme at 1.55 Angstroms, PDB code: 1w6g:

Sodium binding site 1 out of 1 in 1w6g

Go back to Sodium Binding Sites List in 1w6g
Sodium binding site 1 out of 1 in the Agao Holoenzyme at 1.55 Angstroms


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Agao Holoenzyme at 1.55 Angstroms within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na703

b:35.5
occ:1.00
OD1 A:ASP440 2.5 10.8 1.0
O A:MET441 2.5 5.1 1.0
O A:ILE582 2.5 3.7 1.0
OD1 A:ASP581 2.6 10.7 1.0
O A:HOH2334 2.8 29.2 1.0
H A:ILE582 2.9 4.4 1.0
HD1 A:PHE446 3.1 9.6 1.0
H A:MET441 3.1 4.4 1.0
N A:ILE582 3.3 4.0 1.0
N A:MET441 3.3 4.3 1.0
HH21 A:ARG49 3.4 13.0 1.0
C A:ILE582 3.4 3.5 1.0
C A:MET441 3.5 3.1 1.0
HA A:ASP581 3.6 6.3 1.0
CG A:ASP440 3.7 6.0 1.0
CG A:ASP581 3.8 10.2 1.0
C A:ASP440 3.8 4.3 1.0
HB2 A:MET441 3.8 4.1 1.0
C A:ASP581 3.8 5.0 1.0
HH22 A:ARG49 3.8 13.0 1.0
HA A:ASP440 3.9 4.1 1.0
HE1 A:PHE446 3.9 11.7 1.0
CD1 A:PHE446 3.9 8.8 1.0
CA A:ILE582 3.9 4.5 1.0
CA A:MET441 3.9 4.6 1.0
NH2 A:ARG49 3.9 10.4 1.0
HB2 A:TYR546 4.0 6.5 1.0
HG21 A:VAL583 4.1 5.2 1.0
CA A:ASP581 4.1 6.7 1.0
CA A:ASP440 4.3 4.4 1.0
CE1 A:PHE446 4.3 11.6 1.0
CB A:MET441 4.4 2.9 1.0
O A:ASP440 4.5 5.0 1.0
OD2 A:ASP440 4.5 7.9 1.0
HA A:ILE582 4.5 4.3 1.0
HA A:VAL583 4.6 4.1 1.0
N A:VAL583 4.6 4.5 1.0
CB A:ASP581 4.6 7.1 1.0
HG22 A:VAL583 4.6 5.2 1.0
CB A:ASP440 4.6 3.3 1.0
HA A:PHE446 4.6 6.1 1.0
HG13 A:ILE582 4.6 8.4 1.0
HG12 A:ILE582 4.7 8.4 1.0
O A:ASP581 4.7 4.1 1.0
HA A:ALA442 4.7 4.3 1.0
HB2 A:ALA442 4.7 4.4 1.0
OD2 A:ASP581 4.7 15.5 1.0
N A:ALA442 4.7 3.4 1.0
CG2 A:VAL583 4.8 5.6 1.0
HA A:MET441 4.8 3.9 1.0
HB3 A:ASN273 4.9 3.7 1.0
CB A:TYR546 4.9 5.9 1.0
HB3 A:PHE446 4.9 6.6 1.0
HB3 A:TYR546 4.9 6.5 1.0
O A:PHE446 5.0 7.0 1.0
CG1 A:ILE582 5.0 8.4 1.0

Reference:

D.B.Langley, A.P.Duff, H.C.Freeman, J.M.Guss. The Copper Containing Amine Oxidase From Arthrobacter Globiformis: Refinement at 1.55 and 2.20 A Resolution in Two Crystal Forms. Acta Crystallogr.,Sect.F V. 62 1052 2006.
ISSN: ESSN 1744-3091
PubMed: 17077478
DOI: 10.1107/S1744309106038814
Page generated: Tue Dec 15 05:41:01 2020

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