Cadmium in PDB 4ykf: Crystal Structure of the Alkylhydroperoxide Reductase Subunit F (Ahpf) with Nadh From Escherichia Coli

The structure of Crystal Structure of the Alkylhydroperoxide Reductase Subunit F (Ahpf) with Nadh From Escherichia Coli, PDB code: 4ykf was solved by N.Kamariah, M.S.S.Manimekalai, G.Gruber, F.Eisenhaber, B.Eisenhaber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 2.50
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	107.090, 59.390, 121.350, 90.00, 111.34, 90.00
R / Rfree (%)	22.5 / 28.8

The binding sites of Cadmium atom in the Crystal Structure of the Alkylhydroperoxide Reductase Subunit F (Ahpf) with Nadh From Escherichia Coli (pdb code 4ykf). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total only one binding site of Cadmium was determined in the Crystal Structure of the Alkylhydroperoxide Reductase Subunit F (Ahpf) with Nadh From Escherichia Coli, PDB code: 4ykf:

Cadmium binding site 1 out of 1 in the Crystal Structure of the Alkylhydroperoxide Reductase Subunit F (Ahpf) with Nadh From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Crystal Structure of the Alkylhydroperoxide Reductase Subunit F (Ahpf) with Nadh From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Cd603 b:75.0 occ:1.00 ND1 A:HIS130 2.5 77.3 1.0 NE2 A:HIS85 2.6 58.0 1.0 CE1 A:HIS130 3.2 76.5 1.0 CD2 A:HIS85 3.4 57.4 1.0 CG A:HIS130 3.5 74.0 1.0 CE1 A:HIS85 3.6 58.1 1.0 CB A:HIS130 3.9 69.1 1.0 NE2 A:HIS130 4.3 76.0 1.0 CD2 A:HIS130 4.4 74.5 1.0 CA A:HIS130 4.6 67.0 1.0 CG A:HIS85 4.6 55.3 1.0 ND1 A:HIS85 4.7 56.5 1.0

N.Kamariah, M.S.S.Manimekalai, W.Nartey, F.Eisenhaber, B.Eisenhaber, G.Gruber. Crystallographic and Solution Studies of Nad(+)- and Nadh-Bound Alkylhydroperoxide Reductase Subunit F (Ahpf) From Escherichia Coli Provide Insight Into Sequential Enzymatic Steps Biochim.Biophys.Acta V.1847 1139 2015.
ISSN: ISSN 0006-3002
PubMed: 26092085
DOI: 10.1016/J.BBABIO.2015.06.011