Zinc in PDB 1caz: Wild-Type and E106Q Mutant Carbonic Anhydrase Complexed with Acetate

All present enzymatic activity of Wild-Type and E106Q Mutant Carbonic Anhydrase Complexed with Acetate:
4.2.1.1;

The structure of Wild-Type and E106Q Mutant Carbonic Anhydrase Complexed with Acetate, PDB code: 1caz was solved by K.Hakansson, C.Briand, V.Zaitsev, Y.Xue, A.Liljas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 1.90
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Zinc atom in the Wild-Type and E106Q Mutant Carbonic Anhydrase Complexed with Acetate (pdb code 1caz). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Wild-Type and E106Q Mutant Carbonic Anhydrase Complexed with Acetate, PDB code: 1caz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Wild-Type and E106Q Mutant Carbonic Anhydrase Complexed with Acetate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Wild-Type and E106Q Mutant Carbonic Anhydrase Complexed with Acetate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:6.6 occ:1.00 NE2 A:HIS94 2.1 2.1 1.0 OXT A:ACY500 2.1 20.0 1.0 ND1 A:HIS119 2.2 2.7 1.0 NE2 A:HIS96 2.2 2.0 1.0 O A:HOH318 2.6 14.4 1.0 C A:ACY500 2.9 18.6 1.0 CE1 A:HIS119 3.0 3.4 1.0 CD2 A:HIS94 3.1 2.9 1.0 CE1 A:HIS94 3.1 3.3 1.0 CD2 A:HIS96 3.1 2.0 1.0 CE1 A:HIS96 3.2 3.8 1.0 CG A:HIS119 3.2 4.6 1.0 CB A:HIS119 3.6 3.0 1.0 CH3 A:ACY500 3.7 18.4 1.0 OG1 A:THR199 3.8 4.7 1.0 O A:ACY500 4.0 18.8 1.0 NE2 A:HIS119 4.1 4.1 1.0 ND1 A:HIS94 4.2 2.2 1.0 CG A:HIS94 4.2 2.1 1.0 CD2 A:HIS119 4.2 3.0 1.0 CG A:HIS96 4.3 2.0 1.0 ND1 A:HIS96 4.3 3.4 1.0 O A:HOH292 4.6 15.1 1.0

Zinc binding site 2 out of 2 in the Wild-Type and E106Q Mutant Carbonic Anhydrase Complexed with Acetate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Wild-Type and E106Q Mutant Carbonic Anhydrase Complexed with Acetate within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn362 b:78.5 occ:1.00 O A:HOH491 2.3 42.3 1.0 O A:HOH448 2.5 26.8 1.0 O A:VAL135 2.9 9.9 1.0 CB A:CYS206 3.2 5.0 0.2 CB A:CYS206 3.2 3.1 0.8 C A:GLN136 3.3 10.6 1.0 O A:GLN137 3.3 6.4 1.0 N A:GLN137 3.3 9.5 1.0 C A:GLN137 3.5 8.4 1.0 O A:GLN136 3.6 11.9 1.0 O A:HOH331 3.7 14.1 1.0 CA A:GLN136 3.7 9.3 1.0 O A:GLU205 3.7 4.5 1.0 C A:VAL135 3.8 9.1 1.0 CA A:CYS206 3.8 4.4 1.0 C A:GLU205 3.9 4.1 1.0 CA A:GLN137 3.9 9.1 1.0 N A:CYS206 4.0 4.2 1.0 N A:GLN136 4.1 9.1 1.0 N A:PRO138 4.2 8.6 1.0 O A:HOH365 4.3 24.2 1.0 SG A:CYS206 4.3 6.6 0.2 N A:GLU205 4.4 2.9 1.0 CB A:LEU204 4.6 7.9 1.0 SG A:CYS206 4.6 5.6 0.8 CA A:PRO138 4.6 8.8 1.0 CA A:GLU205 4.7 3.4 1.0 C A:LEU204 4.9 4.6 1.0 CA A:VAL135 5.0 8.4 1.0

K.Hakansson, C.Briand, V.Zaitsev, Y.Xue, A.Liljas. Wild-Type and E106Q Mutant Carbonic Anhydrase Complexed with Acetate. Acta Crystallogr.,Sect.D V. 50 101 1994.
ISSN: ISSN 0907-4449
PubMed: 15299482
DOI: 10.1107/S0907444993009667