Zinc in PDB 9l33: Zn-Carbonic Anhydrase II Complexed with 3NPA at 200 K

All present enzymatic activity of Zn-Carbonic Anhydrase II Complexed with 3NPA at 200 K:
4.2.1.1;

The structure of Zn-Carbonic Anhydrase II Complexed with 3NPA at 200 K, PDB code: 9l33 was solved by C.U.Kim, J.K.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.35
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.083, 41.418, 72.21, 90, 104.32, 90
R / Rfree (%)	13.4 / 17.6

The binding sites of Zinc atom in the Zn-Carbonic Anhydrase II Complexed with 3NPA at 200 K (pdb code 9l33). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Zn-Carbonic Anhydrase II Complexed with 3NPA at 200 K, PDB code: 9l33:

Zinc binding site 1 out of 1 in the Zn-Carbonic Anhydrase II Complexed with 3NPA at 200 K


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Zn-Carbonic Anhydrase II Complexed with 3NPA at 200 K within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:6.5 occ:1.00 O A:HOH412 1.9 9.5 1.0 NE2 A:HIS94 2.0 6.2 1.0 NE2 A:HIS96 2.0 6.5 1.0 ND1 A:HIS119 2.0 5.1 1.0 CE1 A:HIS119 2.9 4.8 1.0 CD2 A:HIS94 2.9 7.9 1.0 CD2 A:HIS96 3.0 6.3 1.0 CE1 A:HIS96 3.0 7.1 1.0 CE1 A:HIS94 3.1 6.6 1.0 CG A:HIS119 3.1 4.9 1.0 CB A:HIS119 3.5 5.5 1.0 OG1 A:THR199 3.7 6.7 1.0 O A:HOH489 3.8 11.6 1.0 OE1 A:GLU106 3.9 6.3 1.0 NE2 A:HIS119 4.0 6.1 1.0 CG A:HIS94 4.1 7.3 1.0 ND1 A:HIS96 4.1 7.0 1.0 CG A:HIS96 4.1 6.0 1.0 ND1 A:HIS94 4.1 7.2 1.0 CD2 A:HIS119 4.2 5.6 1.0 O3' A:MNP302 4.2 21.3 1.0 O A:HOH570 4.5 22.4 1.0 O4' A:MNP302 4.6 20.1 1.0 N3' A:MNP302 4.6 16.9 1.0 CD A:GLU106 4.8 6.4 1.0 CA A:HIS119 5.0 4.3 1.0

C.U.Kim, J.K.Kim. Temperature Series of Human Carbonic Anhydrase II with Photolysis of Caged CO2 To Be Published.