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

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

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 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

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