Zinc in PDB 9l31: Zn-Carbonic Anhydrase II Complexed with 3NPA at 160 K

All present enzymatic activity of Zn-Carbonic Anhydrase II Complexed with 3NPA at 160 K:
4.2.1.1;

The structure of Zn-Carbonic Anhydrase II Complexed with 3NPA at 160 K, PDB code: 9l31 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 / 1.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.948, 41.199, 72.246, 90, 104.32, 90
R / Rfree (%)	14.4 / 17.8

The binding sites of Zinc atom in the Zn-Carbonic Anhydrase II Complexed with 3NPA at 160 K (pdb code 9l31). 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 160 K, PDB code: 9l31:

Zinc binding site 1 out of 1 in the Zn-Carbonic Anhydrase II Complexed with 3NPA at 160 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 160 K within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:6.8 occ:1.00 O A:HOH422 1.9 10.2 1.0 NE2 A:HIS96 2.0 6.8 1.0 NE2 A:HIS94 2.0 7.0 1.0 ND1 A:HIS119 2.0 5.3 1.0 CE1 A:HIS119 2.9 5.8 1.0 CD2 A:HIS94 2.9 7.9 1.0 CD2 A:HIS96 3.0 6.0 1.0 CE1 A:HIS96 3.0 7.5 1.0 CE1 A:HIS94 3.1 7.4 1.0 CG A:HIS119 3.1 5.5 1.0 CB A:HIS119 3.6 5.8 1.0 OG1 A:THR199 3.7 7.1 1.0 O A:HOH521 3.7 13.3 1.0 OE1 A:GLU106 3.9 6.7 1.0 NE2 A:HIS119 4.1 6.5 1.0 ND1 A:HIS96 4.1 7.2 1.0 CG A:HIS96 4.1 6.1 1.0 CG A:HIS94 4.1 8.1 1.0 ND1 A:HIS94 4.1 7.6 1.0 O3' A:MNP302 4.1 22.1 1.0 CD2 A:HIS119 4.2 6.1 1.0 O A:HOH592 4.4 23.4 1.0 O4' A:MNP302 4.5 21.7 1.0 N3' A:MNP302 4.6 17.8 1.0 CD A:GLU106 4.8 6.2 1.0

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