Atomistry » Zinc » PDB 2a25-2aer » 2a3l
Atomistry »
  Zinc »
    PDB 2a25-2aer »
      2a3l »

Zinc in PDB 2a3l: X-Ray Structure of Adenosine 5'-Monophosphate Deaminase From Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate

Protein crystallography data

The structure of X-Ray Structure of Adenosine 5'-Monophosphate Deaminase From Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate, PDB code: 2a3l was solved by B.W.Han, G.E.Wesenberg, G.N.Phillips Jr., E.Bitto, C.A.Bingman, S.T.M.Allard, Center For Eukaryotic Structural Genomics (Cesg), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.91 / 3.34
Space group P 62 2 2
Cell size a, b, c (Å), α, β, γ (°) 131.325, 131.325, 208.254, 90.00, 90.00, 120.00
R / Rfree (%) 23.7 / 32.3

Zinc Binding Sites:

The binding sites of Zinc atom in the X-Ray Structure of Adenosine 5'-Monophosphate Deaminase From Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate (pdb code 2a3l). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the X-Ray Structure of Adenosine 5'-Monophosphate Deaminase From Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate, PDB code: 2a3l:

Zinc binding site 1 out of 1 in 2a3l

Go back to Zinc Binding Sites List in 2a3l
Zinc binding site 1 out of 1 in the X-Ray Structure of Adenosine 5'-Monophosphate Deaminase From Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of X-Ray Structure of Adenosine 5'-Monophosphate Deaminase From Arabidopsis Thaliana in Complex with Coformycin 5'-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn840

b:1.0
occ:1.00
O8 A:CF5841 1.8 75.9 1.0
NE2 A:HIS659 2.0 22.9 1.0
NE2 A:HIS393 2.1 52.7 1.0
NE2 A:HIS391 2.1 70.4 1.0
OD2 A:ASP736 2.3 64.3 1.0
N4 A:CF5841 2.7 75.9 1.0
CE1 A:HIS391 2.7 70.4 1.0
CE1 A:HIS659 2.8 22.9 1.0
CD2 A:HIS393 2.9 52.7 1.0
C10 A:CF5841 3.0 75.9 1.0
CE1 A:HIS393 3.1 52.7 1.0
CD2 A:HIS659 3.1 22.9 1.0
C8 A:CF5841 3.1 75.9 1.0
C5 A:CF5841 3.2 75.9 1.0
CD2 A:HIS391 3.2 70.4 1.0
C9 A:CF5841 3.3 75.9 1.0
CG A:ASP736 3.5 64.3 1.0
ND1 A:HIS391 3.9 70.4 1.0
N6 A:CF5841 4.0 75.9 1.0
ND1 A:HIS659 4.0 22.9 1.0
N3 A:CF5841 4.0 75.9 1.0
CG A:HIS393 4.1 52.7 1.0
C7 A:CF5841 4.1 75.9 1.0
ND1 A:HIS393 4.1 52.7 1.0
CG A:HIS659 4.2 22.9 1.0
OD1 A:ASP736 4.2 64.3 1.0
CG A:HIS391 4.2 70.4 1.0
NE2 A:HIS681 4.2 38.0 1.0
N1 A:CF5841 4.2 75.9 1.0
OH A:TYR467 4.5 87.3 1.0
C2 A:CF5841 4.6 75.9 1.0
CB A:ASP736 4.7 64.3 1.0
CA A:ASP736 4.7 60.2 1.0
C1S A:CF5841 4.8 75.9 1.0
CD2 A:HIS681 4.9 38.0 1.0

Reference:

B.W.Han, C.A.Bingman, D.K.Mahnke, R.M.Bannen, S.Y.Bednarek, R.L.Sabina, G.N.Phillips. Membrane Association, Mechanism of Action, and Structure of Arabidopsis Embryonic Factor 1 (FAC1). J.Biol.Chem. V. 281 14939 2006.
ISSN: ISSN 0021-9258
PubMed: 16543243
DOI: 10.1074/JBC.M513009200
Page generated: Wed Dec 16 03:16:32 2020

Last articles

Zn in 8WB0
Zn in 8WAX
Zn in 8WAU
Zn in 8WAZ
Zn in 8WAY
Zn in 8WAV
Zn in 8WAW
Zn in 8WAT
Zn in 8W7M
Zn in 8WD3
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy