Zinc in PDB 9jww: T200H Carbonic Anhydrase II pH 7.8 20 Atm CO2

All present enzymatic activity of T200H Carbonic Anhydrase II pH 7.8 20 Atm CO2:
4.2.1.1; 4.2.1.69;

The structure of T200H Carbonic Anhydrase II pH 7.8 20 Atm CO2, PDB code: 9jww was solved by S.W.Lim, C.U.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.32 / 1.25
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	42.659, 41.668, 72.587, 90, 104.68, 90
R / Rfree (%)	13.7 / 15.9

The binding sites of Zinc atom in the T200H Carbonic Anhydrase II pH 7.8 20 Atm CO2 (pdb code 9jww). 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 T200H Carbonic Anhydrase II pH 7.8 20 Atm CO2, PDB code: 9jww:

Zinc binding site 1 out of 1 in the T200H Carbonic Anhydrase II pH 7.8 20 Atm CO2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of T200H Carbonic Anhydrase II pH 7.8 20 Atm CO2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn301 b:6.5 occ:1.00 O A:HOH517 1.9 9.9 1.0 NE2 A:HIS96 2.0 6.4 1.0 NE2 A:HIS94 2.0 6.3 1.0 ND1 A:HIS119 2.0 5.9 1.0 CE1 A:HIS119 2.9 6.1 1.0 CD2 A:HIS94 3.0 7.0 1.0 CE1 A:HIS94 3.0 6.5 1.0 CD2 A:HIS96 3.0 5.7 1.0 CE1 A:HIS96 3.0 7.1 1.0 CG A:HIS119 3.1 5.7 1.0 O A:HOH609 3.2 21.0 1.0 O2 A:CO2302 3.4 14.4 1.0 CB A:HIS119 3.6 5.7 1.0 C A:CO2302 3.6 16.1 1.0 O A:HOH461 3.9 15.5 1.0 OG1 A:THR199 4.0 7.3 1.0 OE1 A:GLU106 4.0 7.4 1.0 NE2 A:HIS119 4.1 6.3 1.0 CG A:HIS94 4.1 6.7 1.0 ND1 A:HIS94 4.1 6.8 1.0 O A:HOH625 4.1 15.1 1.0 ND1 A:HIS96 4.2 7.5 1.0 CG A:HIS96 4.2 6.0 1.0 CD2 A:HIS119 4.2 6.1 1.0 O1 A:CO2302 4.2 18.7 1.0 O A:HOH604 4.2 21.4 1.0 CD A:GLU106 4.9 7.4 1.0

S.W.Lim, H.Jeong, G.H.Kim, D.Min, J.K.Kim, C.U.Kim. Conformational Flexibility of HIS200 Enables Catalytic Activity in the T200H Mutant of Carbonic Anhydrase II. Mol.Cells V. 48 00226 2025.
ISSN: ISSN 1016-8478
PubMed: 40441537
DOI: 10.1016/J.MOCELL.2025.100226