Zinc in PDB 3kve: Structure of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization of the Quaternary Structure By Divalent Ions and Structural Changes in the Dynamic Active Site

The structure of Structure of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization of the Quaternary Structure By Divalent Ions and Structural Changes in the Dynamic Active Site, PDB code: 3kve was solved by D.Gergiova, M.T.Murakami, M.Perbandt, R.K.Arni, C.Betzel, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.40 / 2.57
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	196.978, 95.839, 108.442, 90.00, 92.53, 90.00
R / Rfree (%)	19.1 / 27.6

The binding sites of Zinc atom in the Structure of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization of the Quaternary Structure By Divalent Ions and Structural Changes in the Dynamic Active Site (pdb code 3kve). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structure of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization of the Quaternary Structure By Divalent Ions and Structural Changes in the Dynamic Active Site, PDB code: 3kve:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in the Structure of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization of the Quaternary Structure By Divalent Ions and Structural Changes in the Dynamic Active Site


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization of the Quaternary Structure By Divalent Ions and Structural Changes in the Dynamic Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn489 b:19.9 occ:1.00 ND1 A:HIS75 2.2 12.2 1.0 O D:HOH490 2.3 2.0 1.0 OE2 D:GLU279 2.4 26.8 1.0 OE1 D:GLU279 2.6 25.6 1.0 O D:HOH491 2.6 11.4 1.0 CD D:GLU279 2.9 27.7 1.0 CE1 A:HIS75 3.1 10.8 1.0 CG A:HIS75 3.2 12.2 1.0 CB A:HIS75 3.5 12.7 1.0 CA A:HIS75 3.8 13.1 1.0 CE A:MET416 4.2 17.9 1.0 NE2 A:HIS75 4.3 10.4 1.0 CD2 A:HIS75 4.3 10.8 1.0 CG D:GLU279 4.4 27.4 1.0 N A:ARG76 4.4 14.0 1.0 C A:HIS75 4.7 13.7 1.0 O A:ARG76 4.9 14.8 1.0 N A:HIS75 4.9 12.2 1.0

Zinc binding site 2 out of 4 in the Structure of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization of the Quaternary Structure By Divalent Ions and Structural Changes in the Dynamic Active Site


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization of the Quaternary Structure By Divalent Ions and Structural Changes in the Dynamic Active Site within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn489 b:19.1 occ:1.00 OE2 C:GLU279 2.1 32.5 1.0 ND1 B:HIS75 2.2 16.5 1.0 O C:HOH490 2.2 2.0 1.0 O C:HOH491 2.4 9.1 1.0 CD C:GLU279 2.8 31.3 1.0 OE1 C:GLU279 2.8 32.1 1.0 CE1 B:HIS75 3.1 16.6 1.0 CG B:HIS75 3.2 14.9 1.0 CB B:HIS75 3.6 13.4 1.0 CA B:HIS75 3.8 13.2 1.0 CG C:GLU279 4.2 31.0 1.0 NE2 B:HIS75 4.2 16.9 1.0 CD2 B:HIS75 4.3 15.5 1.0 CE B:MET416 4.5 20.6 1.0 N B:ARG76 4.5 13.8 1.0 C B:HIS75 4.7 13.5 1.0 SD B:MET416 4.9 20.5 1.0 N B:HIS75 4.9 12.9 1.0 NH1 B:ARG67 4.9 23.7 1.0 O B:ARG76 5.0 14.4 1.0

Zinc binding site 3 out of 4 in the Structure of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization of the Quaternary Structure By Divalent Ions and Structural Changes in the Dynamic Active Site


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization of the Quaternary Structure By Divalent Ions and Structural Changes in the Dynamic Active Site within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn489 b:29.1 occ:1.00 OE2 B:GLU279 1.9 31.1 1.0 ND1 C:HIS75 1.9 17.3 1.0 O C:HOH492 2.2 2.0 1.0 CD B:GLU279 2.6 32.3 1.0 OE1 B:GLU279 2.7 35.0 1.0 CE1 C:HIS75 2.7 17.4 1.0 CG C:HIS75 3.0 16.7 1.0 CB C:HIS75 3.5 16.2 1.0 CA C:HIS75 3.8 16.4 1.0 NE2 C:HIS75 3.9 17.0 1.0 CD2 C:HIS75 4.0 16.8 1.0 CG B:GLU279 4.1 32.7 1.0 N C:ARG76 4.5 17.6 1.0 C C:HIS75 4.7 17.1 1.0 CE C:MET416 4.7 20.6 1.0 SD C:MET416 4.8 23.3 1.0 NH2 C:ARG67 4.9 31.1 1.0 O C:ARG76 4.9 18.8 1.0 N C:HIS75 5.0 15.4 1.0

Zinc binding site 4 out of 4 in the Structure of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization of the Quaternary Structure By Divalent Ions and Structural Changes in the Dynamic Active Site


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization of the Quaternary Structure By Divalent Ions and Structural Changes in the Dynamic Active Site within 5.0Å range: probe atom residue distance (Å) B Occ D:Zn489 b:22.6 occ:1.00 ND1 D:HIS75 1.9 18.7 1.0 OE2 A:GLU279 2.2 32.2 1.0 O A:HOH493 2.4 2.0 1.0 OE1 A:GLU279 2.6 31.3 1.0 CD A:GLU279 2.7 31.6 1.0 CE1 D:HIS75 2.9 18.6 1.0 CG D:HIS75 3.0 16.6 1.0 CB D:HIS75 3.4 14.5 1.0 CA D:HIS75 3.7 14.6 1.0 CE D:MET416 3.8 23.8 1.0 NE2 D:HIS75 4.0 20.0 1.0 CD2 D:HIS75 4.1 18.0 1.0 CG A:GLU279 4.2 31.7 1.0 N D:ARG76 4.6 14.4 1.0 C D:HIS75 4.7 14.6 1.0 N D:HIS75 4.8 14.1 1.0 O D:ARG76 4.9 14.2 1.0

D.Gergiova, M.T.Murakami, M.Perbandt, R.K.Arni, C.Betzel. Structure of Native L-Amino Acid Oxidase From Vipera Ammodytes Ammodytes: Stabilization of the Quaternary Structure By Divalent Ions and Structural Changes in the Dynamic Active Site To Be Published.