Zinc in PDB 5akq: X-Ray Structure and Mutagenesis Studies of the N- Isopropylammelide Isopropylaminohydrolase, Atzc

All present enzymatic activity of X-Ray Structure and Mutagenesis Studies of the N- Isopropylammelide Isopropylaminohydrolase, Atzc:
3.5.99.4;

The structure of X-Ray Structure and Mutagenesis Studies of the N- Isopropylammelide Isopropylaminohydrolase, Atzc, PDB code: 5akq was solved by S.Balotra, A.C.Warden, J.Newman, L.J.Briggs, C.Scott, T.S.Peat, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	110.50 / 2.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	106.204, 86.581, 114.066, 90.00, 104.36, 90.00
R / Rfree (%)	20.451 / 24.129

The structure of X-Ray Structure and Mutagenesis Studies of the N- Isopropylammelide Isopropylaminohydrolase, Atzc also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Zinc atom in the X-Ray Structure and Mutagenesis Studies of the N- Isopropylammelide Isopropylaminohydrolase, Atzc (pdb code 5akq). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the X-Ray Structure and Mutagenesis Studies of the N- Isopropylammelide Isopropylaminohydrolase, Atzc, PDB code: 5akq:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the X-Ray Structure and Mutagenesis Studies of the N- Isopropylammelide Isopropylaminohydrolase, Atzc


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 and Mutagenesis Studies of the N- Isopropylammelide Isopropylaminohydrolase, Atzc within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn1405 b:33.6 occ:1.00 NE2 A:HIS60 2.1 22.6 1.0 NE2 A:HIS62 2.1 30.9 1.0 NE2 A:HIS217 2.2 23.2 1.0 OD1 A:ASP303 2.9 32.0 1.0 CE1 A:HIS62 3.0 31.2 1.0 CE1 A:HIS60 3.0 23.5 1.0 CD2 A:HIS217 3.1 25.0 1.0 CE1 A:HIS217 3.2 22.5 1.0 CD2 A:HIS60 3.2 23.6 1.0 CD2 A:HIS62 3.3 30.3 1.0 NE2 A:HIS249 3.8 24.5 1.0 CG A:ASP303 4.0 33.5 1.0 ND1 A:HIS62 4.1 30.7 1.0 ND1 A:HIS60 4.2 21.6 1.0 CG A:HIS217 4.2 24.8 1.0 ND1 A:HIS217 4.2 24.3 1.0 CG A:HIS60 4.3 21.6 1.0 CG A:HIS62 4.3 28.4 1.0 OD1 A:ASP304 4.3 24.5 1.0 OD2 A:ASP303 4.4 35.4 1.0 CE1 A:HIS249 4.5 21.9 1.0 CD2 A:HIS249 4.7 22.8 1.0 CD2 A:HIS125 5.0 20.4 1.0

Zinc binding site 2 out of 2 in the X-Ray Structure and Mutagenesis Studies of the N- Isopropylammelide Isopropylaminohydrolase, Atzc


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of X-Ray Structure and Mutagenesis Studies of the N- Isopropylammelide Isopropylaminohydrolase, Atzc within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn1405 b:32.7 occ:1.00 NE2 B:HIS60 2.1 22.6 1.0 NE2 B:HIS62 2.2 24.1 1.0 NE2 B:HIS217 2.3 32.0 1.0 OD1 B:ASP303 2.7 27.8 1.0 CE1 B:HIS60 3.0 23.2 1.0 CE1 B:HIS62 3.0 22.9 1.0 CD2 B:HIS60 3.1 22.6 1.0 CD2 B:HIS217 3.1 32.8 1.0 CE1 B:HIS217 3.3 32.9 1.0 CD2 B:HIS62 3.3 24.3 1.0 NE2 B:HIS249 3.7 27.8 1.0 CG B:ASP303 3.7 26.5 1.0 OD2 B:ASP303 4.0 31.7 1.0 ND1 B:HIS60 4.1 21.8 1.0 ND1 B:HIS62 4.2 23.3 1.0 CG B:HIS60 4.2 21.4 1.0 CG B:HIS217 4.3 30.8 1.0 ND1 B:HIS217 4.3 31.9 1.0 OD1 B:ASP304 4.3 26.6 1.0 CG B:HIS62 4.3 24.1 1.0 CE1 B:HIS249 4.5 26.1 1.0 CD2 B:HIS249 4.6 26.0 1.0

S.Balotra, A.C.Warden, J.Newman, L.J.Briggs, C.Scott, T.S.Peat. X-Ray Structure and Mutagenesis Studies of the N- Isopropylammelide Isopropylaminohydrolase, Atzc To Be Published.