Zinc in PDB 1j9w: Solution Structure of the Cai Michigan 1 Variant

All present enzymatic activity of Solution Structure of the Cai Michigan 1 Variant:
4.2.1.1;

The structure of Solution Structure of the Cai Michigan 1 Variant, PDB code: 1j9w was solved by F.Briganti, M.Ferraroni, W.R.Chedwiggen, A.Scozzafava, C.T.Supuran, S.Tilli, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	15.00 / 2.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	61.875, 71.732, 120.392, 90.00, 90.00, 90.00
R / Rfree (%)	20.5 / 31.1

The binding sites of Zinc atom in the Solution Structure of the Cai Michigan 1 Variant (pdb code 1j9w). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Solution Structure of the Cai Michigan 1 Variant, PDB code: 1j9w:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Solution Structure of the Cai Michigan 1 Variant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Solution Structure of the Cai Michigan 1 Variant within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn261 b:16.8 occ:1.00 O1 A:EDO401 1.7 16.0 1.0 NE2 A:HIS94 1.9 13.8 1.0 ND1 A:HIS119 2.2 15.0 1.0 NE2 A:HIS96 2.2 19.2 1.0 CE1 A:HIS94 2.7 13.8 1.0 CD2 A:HIS94 3.0 13.3 1.0 CD2 A:HIS96 3.0 18.7 1.0 CE1 A:HIS119 3.0 14.0 1.0 O2 A:EDO401 3.1 14.2 1.0 CG A:HIS119 3.2 15.8 1.0 C1 A:EDO401 3.2 15.4 1.0 CE1 A:HIS96 3.3 18.7 1.0 CB A:HIS119 3.6 16.1 1.0 C2 A:EDO401 3.7 13.5 1.0 OG1 A:THR199 3.8 19.6 1.0 ND1 A:HIS94 3.9 13.2 1.0 CG A:HIS94 4.0 13.6 1.0 NE2 A:HIS119 4.2 14.6 1.0 CG A:HIS96 4.2 18.8 1.0 OE1 A:GLU106 4.3 8.0 1.0 CD2 A:HIS119 4.3 15.4 1.0 ND1 A:HIS96 4.3 18.7 1.0 O A:HOH407 4.5 3.2 1.0 CA A:HIS119 5.0 17.9 1.0 O A:HOH441 5.0 30.9 1.0

Zinc binding site 2 out of 2 in the Solution Structure of the Cai Michigan 1 Variant


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Solution Structure of the Cai Michigan 1 Variant within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn262 b:18.5 occ:1.00 O2 B:EDO402 1.7 9.0 1.0 NE2 B:HIS94 1.9 12.8 1.0 NE2 B:HIS96 2.0 14.8 1.0 ND1 B:HIS119 2.0 16.4 1.0 CE1 B:HIS119 2.8 16.4 1.0 CE1 B:HIS94 2.8 12.8 1.0 CD2 B:HIS96 3.0 14.9 1.0 CD2 B:HIS94 3.0 12.7 1.0 CE1 B:HIS96 3.0 15.5 1.0 CG B:HIS119 3.1 17.2 1.0 C2 B:EDO402 3.2 8.4 1.0 O1 B:EDO402 3.6 7.0 1.0 CB B:HIS119 3.6 16.9 1.0 OG1 B:THR199 3.7 15.0 1.0 C1 B:EDO402 3.8 7.0 1.0 NE2 B:HIS119 3.8 16.8 1.0 ND1 B:HIS94 4.0 12.1 1.0 CD2 B:HIS119 4.0 16.8 1.0 CG B:HIS94 4.1 12.8 1.0 OE1 B:GLU106 4.1 11.7 1.0 CG B:HIS96 4.1 15.2 1.0 ND1 B:HIS96 4.1 14.8 1.0 O B:HOH410 4.5 13.7 1.0 O B:HOH415 4.7 8.4 1.0 CB B:THR199 5.0 15.8 1.0

M.Ferraroni, S.Tilli, F.Briganti, W.R.Chegwidden, C.T.Supuran, K.E.Wiebauer, R.E.Tashian, A.Scozzafava. Crystal Structure of A Zinc-Activated Variant of Human Carbonic Anhydrase I, Ca I Michigan 1: Evidence For A Second Zinc Binding Site Involving Arginine Coordination. Biochemistry V. 41 6237 2002.
ISSN: ISSN 0006-2960
PubMed: 12009884
DOI: 10.1021/BI0120446