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Arsenic in PDB 3et6: The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase

Protein crystallography data

The structure of The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase, PDB code: 3et6 was solved by J.A.Winger, E.R.Derbyshire, M.H.Lamers, M.A.Marletta, J.Kuriyan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 28.00 / 2.55
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 123.678, 123.678, 62.822, 90.00, 90.00, 120.00
R / Rfree (%) 17.2 / 21.5

Arsenic Binding Sites:

The binding sites of Arsenic atom in the The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase (pdb code 3et6). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total 5 binding sites of Arsenic where determined in the The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase, PDB code: 3et6:
Jump to Arsenic binding site number: 1; 2; 3; 4; 5;

Arsenic binding site 1 out of 5 in 3et6

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Arsenic binding site 1 out of 5 in the The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As499

b:91.0
occ:1.00
AS A:CAS499 0.0 91.0 1.0
CE1 A:CAS499 2.0 79.2 1.0
CE2 A:CAS499 2.0 44.9 1.0
SG A:CAS499 2.2 72.6 1.0
CB A:CAS499 3.3 55.0 1.0
SG B:CAS592 3.9 59.9 1.0
CA A:CAS499 3.9 75.4 1.0
O A:CAS499 4.0 66.9 1.0
CB B:PHE594 4.0 47.7 1.0
CG1 B:VAL580 4.1 53.4 1.0
CG B:PHE594 4.2 54.5 1.0
C A:CAS499 4.2 78.3 1.0
CD2 B:PHE594 4.4 63.4 1.0
CD1 B:PHE594 4.7 70.0 1.0
CG1 B:VAL584 4.8 66.9 1.0
CB B:CAS592 4.9 48.5 1.0
CD2 A:LEU502 4.9 55.5 1.0

Arsenic binding site 2 out of 5 in 3et6

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Arsenic binding site 2 out of 5 in the The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 2 of The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As592

b:90.2
occ:1.00
AS A:CAS592 0.0 90.2 1.0
CE1 A:CAS592 1.9 64.4 1.0
CE2 A:CAS592 2.0 0.5 1.0
SG A:CAS592 2.2 86.5 1.0
CB A:CAS592 3.3 59.4 1.0
O B:THR524 3.9 49.7 1.0
CA A:CAS592 3.9 64.0 1.0
N A:LEU593 4.1 68.4 1.0
O A:LEU593 4.2 69.8 1.0
C A:CAS592 4.4 64.3 1.0
CA B:ILE525 4.4 59.5 1.0
C B:THR524 4.4 55.2 1.0
O B:ILE525 4.4 73.8 1.0
N B:ILE525 4.7 55.8 1.0
C B:ILE525 4.7 58.5 1.0
CD1 B:ILE525 4.7 71.1 1.0
C A:LEU593 4.8 66.5 1.0
CD A:ARG590 4.9 95.0 1.0
O B:GLU523 4.9 48.0 1.0
CG2 A:VAL584 5.0 61.8 1.0

Arsenic binding site 3 out of 5 in 3et6

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Arsenic binding site 3 out of 5 in the The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 3 of The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As499

b:0.2
occ:1.00
AS B:CAS499 0.0 0.2 1.0
CE2 B:CAS499 2.0 0.5 1.0
CE1 B:CAS499 2.0 0.8 1.0
SG B:CAS499 2.3 0.2 1.0
CB B:CAS499 3.5 81.6 1.0
SG A:CAS592 4.0 86.5 1.0
CB A:PHE594 4.1 66.3 1.0
CG A:PHE594 4.3 76.5 1.0
O B:CAS499 4.3 0.1 1.0
CA B:CAS499 4.3 95.7 1.0
CG1 A:VAL580 4.5 71.7 1.0
C B:CAS499 4.6 1.0 1.0
CD1 A:PHE594 4.7 87.5 1.0
CD2 A:PHE594 4.8 70.2 1.0
CB A:ALA470 4.8 76.7 1.0
CB A:CAS592 4.9 59.4 1.0
CG1 A:VAL584 4.9 74.0 1.0

Arsenic binding site 4 out of 5 in 3et6

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Arsenic binding site 4 out of 5 in the The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 4 of The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As592

b:75.9
occ:1.00
AS B:CAS592 0.0 75.9 1.0
CE1 B:CAS592 2.0 71.5 1.0
CE2 B:CAS592 2.0 40.9 1.0
SG B:CAS592 2.3 59.9 1.0
CB B:CAS592 3.3 48.5 1.0
CA B:CAS592 3.8 59.3 1.0
N B:LEU593 3.9 36.7 1.0
O B:LEU593 3.9 43.7 1.0
O A:THR524 3.9 46.6 1.0
C B:CAS592 4.2 48.1 1.0
C A:THR524 4.4 57.4 1.0
C B:LEU593 4.5 48.8 1.0
O B:HOH689 4.5 46.1 1.0
CA A:ILE525 4.6 52.8 1.0
N A:ILE525 4.7 49.3 1.0
OD1 A:ASP527 4.8 95.8 1.0
CD1 A:ILE525 4.8 57.3 1.0
CA B:LEU593 4.9 46.4 1.0
CB B:PHE594 4.9 47.7 1.0
CG1 A:ILE525 4.9 57.6 1.0
CG2 B:VAL584 5.0 55.2 1.0

Arsenic binding site 5 out of 5 in 3et6

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Arsenic binding site 5 out of 5 in the The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 5 of The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:As621

b:65.2
occ:1.00
AS B:CAS621 0.0 65.2 1.0
CE2 B:CAS621 2.0 47.5 1.0
CE1 B:CAS621 2.0 0.4 1.0
SG B:CAS621 2.3 52.5 1.0
CB B:CAS621 3.5 17.4 1.0
CA B:CAS621 3.7 30.2 1.0
N B:CAS621 4.2 23.4 1.0
C B:CAS621 4.9 41.0 1.0
CE B:LYS626 4.9 38.4 1.0
O B:GLU617 5.0 35.7 1.0

Reference:

J.A.Winger, E.R.Derbyshire, M.H.Lamers, M.A.Marletta, J.Kuriyan. The Crystal Structure of the Catalytic Domain of A Eukaryotic Guanylate Cyclase. Bmc Struct.Biol. V. 8 42 2008.
ISSN: ESSN 1472-6807
PubMed: 18842118
DOI: 10.1186/1472-6807-8-42
Page generated: Tue Oct 27 16:50:04 2020

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