Nickel in PDB 1k8t: Crystal Structure of the Adenylyl Cyclase Domain of Anthrax Edema Factor (Ef)

All present enzymatic activity of Crystal Structure of the Adenylyl Cyclase Domain of Anthrax Edema Factor (Ef):
4.6.1.1;

The structure of Crystal Structure of the Adenylyl Cyclase Domain of Anthrax Edema Factor (Ef), PDB code: 1k8t was solved by C.L.Drum, S.-Z.Yan, J.Bard, Y.-Q.Shen, D.Lu, S.Soelaiman, Z.Grabarek, A.Bohm, W.-J.Tang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.60
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	50.476, 203.604, 74.034, 90.00, 90.00, 90.00
R / Rfree (%)	22.9 / 27.6

The binding sites of Nickel atom in the Crystal Structure of the Adenylyl Cyclase Domain of Anthrax Edema Factor (Ef) (pdb code 1k8t). This binding sites where shown within 5.0 Angstroms radius around Nickel atom.
In total only one binding site of Nickel was determined in the Crystal Structure of the Adenylyl Cyclase Domain of Anthrax Edema Factor (Ef), PDB code: 1k8t:

Nickel binding site 1 out of 1 in the Crystal Structure of the Adenylyl Cyclase Domain of Anthrax Edema Factor (Ef)


Mono view


Stereo pair view

A full contact list of Nickel with other atoms in the Ni binding site number 1 of Crystal Structure of the Adenylyl Cyclase Domain of Anthrax Edema Factor (Ef) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ni2001 b:79.1 occ:1.00 NE2 A:HIS577 2.4 75.1 1.0 OD2 A:ASP491 2.7 52.3 1.0 OD1 A:ASP493 2.8 55.5 1.0 O A:HOH39 3.0 66.4 1.0 CE1 A:HIS577 3.1 74.5 1.0 O A:HOH67 3.2 58.4 1.0 OD1 A:ASP491 3.3 52.1 1.0 CG A:ASP491 3.4 50.4 1.0 CD2 A:HIS577 3.6 73.7 1.0 CG A:ASP493 3.8 52.5 1.0 OD2 A:ASP493 4.1 58.0 1.0 ND1 A:HIS577 4.3 73.5 1.0 CE A:LYS346 4.6 48.9 1.0 CG A:HIS577 4.6 73.3 1.0 O A:HOH95 4.7 65.0 1.0 CB A:ASP491 4.9 47.6 1.0

C.L.Drum, S.-Z.Yan, J.Bard, Y.-Q.Shen, D.Lu, S.Soelaiman, Z.Grabarek, A.Bohm, W.-J.Tang. Structural Basis For the Activation of Anthrax Adenylyl Cyclase Exotoxin By Calmodulin Nature V. 415 396 2002.
ISSN: ISSN 0028-0836
PubMed: 11807546
DOI: 10.1038/415396A