Zinc in PDB 1thj: Carbonic Anhydrase From Methanosarcina

All present enzymatic activity of Carbonic Anhydrase From Methanosarcina:
4.2.1.1;

The structure of Carbonic Anhydrase From Methanosarcina, PDB code: 1thj was solved by C.Kisker, H.Schindelin, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.80
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	71.840, 71.840, 333.513, 90.00, 90.00, 90.00
R / Rfree (%)	23.4 / 29.5

The binding sites of Zinc atom in the Carbonic Anhydrase From Methanosarcina (pdb code 1thj). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Carbonic Anhydrase From Methanosarcina, PDB code: 1thj:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in the Carbonic Anhydrase From Methanosarcina


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Carbonic Anhydrase From Methanosarcina within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn214 b:41.0 occ:1.00 O C:HOH215 2.0 27.9 1.0 NE2 A:HIS122 2.1 26.4 1.0 ND1 A:HIS81 2.1 33.6 1.0 NE2 C:HIS117 2.1 10.9 1.0 CE1 A:HIS81 2.8 36.4 1.0 CE1 A:HIS122 3.1 29.6 1.0 CD2 A:HIS122 3.1 22.8 1.0 CD2 C:HIS117 3.2 19.6 1.0 CE1 C:HIS117 3.2 27.1 1.0 CG A:HIS81 3.2 29.3 1.0 CB A:HIS81 3.8 23.6 1.0 OE1 C:GLN75 4.1 37.4 1.0 NE2 A:HIS81 4.1 29.0 1.0 OE1 A:GLU62 4.2 52.8 1.0 ND1 A:HIS122 4.2 25.0 1.0 CG A:HIS122 4.2 22.9 1.0 CD2 A:HIS81 4.3 28.4 1.0 ND1 C:HIS117 4.3 20.0 1.0 CG C:HIS117 4.3 14.6 1.0 O A:ALA82 4.3 38.5 1.0 N A:ALA82 4.6 26.2 1.0 C A:HIS81 4.8 24.6 1.0 C A:ALA82 4.8 31.8 1.0 CE C:MET135 4.8 22.4 1.0 CA A:HIS81 4.9 21.3 1.0 CD C:GLN75 5.0 27.7 1.0

Zinc binding site 2 out of 3 in the Carbonic Anhydrase From Methanosarcina


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Carbonic Anhydrase From Methanosarcina within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn214 b:42.0 occ:1.00 O A:HOH215 2.0 25.1 1.0 ND1 B:HIS81 2.0 36.4 1.0 NE2 B:HIS122 2.0 23.7 1.0 NE2 A:HIS117 2.2 25.6 1.0 CE1 B:HIS81 2.8 38.3 1.0 CE1 B:HIS122 3.0 32.5 1.0 CD2 B:HIS122 3.1 22.3 1.0 CD2 A:HIS117 3.2 24.7 1.0 CG B:HIS81 3.2 28.4 1.0 CE1 A:HIS117 3.2 31.1 1.0 CB B:HIS81 3.7 17.7 1.0 OE1 A:GLN75 4.0 35.6 1.0 NE2 B:HIS81 4.1 28.6 1.0 ND1 B:HIS122 4.2 25.6 1.0 CG B:HIS122 4.2 21.3 1.0 OE1 B:GLU62 4.2 49.1 1.0 CD2 B:HIS81 4.2 30.8 1.0 O B:ALA82 4.3 37.0 1.0 ND1 A:HIS117 4.3 24.0 1.0 CG A:HIS117 4.3 19.3 1.0 N B:ALA82 4.6 34.1 1.0 C B:HIS81 4.7 29.8 1.0 CE A:MET135 4.8 24.0 1.0 C B:ALA82 4.8 34.0 1.0 CA B:HIS81 4.9 23.1 1.0 CD A:GLN75 4.9 31.1 1.0

Zinc binding site 3 out of 3 in the Carbonic Anhydrase From Methanosarcina


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Carbonic Anhydrase From Methanosarcina within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn214 b:44.0 occ:1.00 O B:HOH215 2.0 28.8 1.0 ND1 C:HIS81 2.0 33.9 1.0 NE2 C:HIS122 2.0 31.0 1.0 NE2 B:HIS117 2.1 20.2 1.0 CE1 C:HIS81 2.8 37.4 1.0 CE1 C:HIS122 3.1 37.1 1.0 CD2 C:HIS122 3.1 28.6 1.0 CE1 B:HIS117 3.1 32.9 1.0 CD2 B:HIS117 3.1 25.6 1.0 CG C:HIS81 3.2 28.3 1.0 CB C:HIS81 3.7 21.8 1.0 OE1 B:GLN75 4.0 30.6 1.0 NE2 C:HIS81 4.1 26.1 1.0 OE1 C:GLU62 4.2 51.7 1.0 ND1 C:HIS122 4.2 29.0 1.0 CG C:HIS122 4.2 25.7 1.0 CD2 C:HIS81 4.3 26.5 1.0 ND1 B:HIS117 4.3 25.9 1.0 CG B:HIS117 4.3 22.1 1.0 O C:ALA82 4.3 28.9 1.0 N C:ALA82 4.5 19.6 1.0 C C:HIS81 4.7 22.6 1.0 C C:ALA82 4.8 29.3 1.0 CE B:MET135 4.8 22.1 1.0 CA C:HIS81 4.9 17.9 1.0 CD B:GLN75 4.9 26.1 1.0

C.Kisker, H.Schindelin, B.E.Alber, J.G.Ferry, D.C.Rees. A Left-Hand Beta-Helix Revealed By the Crystal Structure of A Carbonic Anhydrase From the Archaeon Methanosarcina Thermophila. Embo J. V. 15 2323 1996.
ISSN: ISSN 0261-4189
PubMed: 8665839