Zinc in PDB 1h4n: H94N Carbonic Anhydrase II Complexed with Tris

All present enzymatic activity of H94N Carbonic Anhydrase II Complexed with Tris:
4.2.1.1;

The structure of H94N Carbonic Anhydrase II Complexed with Tris, PDB code: 1h4n was solved by C.A.Lesburg, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.00
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 (%)	15.4 / 20.7

The binding sites of Zinc atom in the H94N Carbonic Anhydrase II Complexed with Tris (pdb code 1h4n). 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 H94N Carbonic Anhydrase II Complexed with Tris, PDB code: 1h4n:

Zinc binding site 1 out of 1 in the H94N Carbonic Anhydrase II Complexed with Tris


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of H94N Carbonic Anhydrase II Complexed with Tris within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn262 b:11.2 occ:1.00 ND1 A:HIS119 2.0 7.8 1.0 OD1 A:ASN94 2.0 12.2 1.0 NE2 A:HIS96 2.1 5.1 1.0 N A:TRS263 2.3 8.2 1.0 O2 A:TRS263 2.4 10.0 1.0 CE1 A:HIS119 2.9 5.6 1.0 CD2 A:HIS96 3.0 4.5 1.0 CG A:HIS119 3.1 5.6 1.0 CG A:ASN94 3.1 9.9 1.0 C A:TRS263 3.2 9.9 1.0 CE1 A:HIS96 3.2 7.7 1.0 C2 A:TRS263 3.2 10.4 1.0 CB A:HIS119 3.5 4.3 1.0 ND2 A:ASN94 3.6 2.6 1.0 C3 A:TRS263 3.7 10.7 1.0 O A:HOH372 3.7 15.8 1.0 NE2 A:HIS119 4.1 7.0 1.0 CD2 A:HIS119 4.2 6.0 1.0 CG A:HIS96 4.2 7.9 1.0 ND1 A:HIS96 4.3 4.8 1.0 O3 A:TRS263 4.3 11.2 1.0 OE1 A:GLU106 4.4 7.8 1.0 CB A:ASN94 4.4 7.1 1.0 OG1 A:THR199 4.5 7.6 1.0 C1 A:TRS263 4.5 11.2 1.0 O1 A:TRS263 4.6 13.2 1.0 O A:ASN94 4.7 4.2 1.0 C A:ASN94 4.8 7.8 1.0 CA A:HIS119 4.9 4.6 1.0

C.A.Lesburg, C.Huang, D.W.Christianson, C.A.Fierke. Histidine --> Carboxamide Ligand Substitutions in the Zinc Binding Site of Carbonic Anhydrase II Alter Metal Coordination Geometry But Retain Catalytic Activity. Biochemistry V. 36 15780 1997.
ISSN: ISSN 0006-2960
PubMed: 9398308
DOI: 10.1021/BI971296X