Zinc in PDB 1dmy: Complex Between Murine Mitochondrial Carbonic Anyhdrase V and the Transition State Analogue Acetazolamide

All present enzymatic activity of Complex Between Murine Mitochondrial Carbonic Anyhdrase V and the Transition State Analogue Acetazolamide:
4.2.1.1;

The structure of Complex Between Murine Mitochondrial Carbonic Anyhdrase V and the Transition State Analogue Acetazolamide, PDB code: 1dmy was solved by P.A.Boriack-Sjodin, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.45
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	48.690, 60.370, 60.440, 67.65, 75.26, 75.21
R / Rfree (%)	17 / n/a

The binding sites of Zinc atom in the Complex Between Murine Mitochondrial Carbonic Anyhdrase V and the Transition State Analogue Acetazolamide (pdb code 1dmy). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Complex Between Murine Mitochondrial Carbonic Anyhdrase V and the Transition State Analogue Acetazolamide, PDB code: 1dmy:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Complex Between Murine Mitochondrial Carbonic Anyhdrase V and the Transition State Analogue Acetazolamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Complex Between Murine Mitochondrial Carbonic Anyhdrase V and the Transition State Analogue Acetazolamide within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn280 b:22.0 occ:1.00 N1 A:AZM400 1.9 21.7 1.0 NE2 A:HIS96 1.9 2.0 1.0 ND1 A:HIS119 2.0 4.2 1.0 NE2 A:HIS94 2.2 7.9 1.0 CD2 A:HIS94 2.7 5.4 1.0 O1 A:AZM400 2.8 25.0 1.0 CE1 A:HIS119 2.8 8.7 1.0 S1 A:AZM400 2.8 29.3 1.0 CD2 A:HIS96 2.9 3.9 1.0 CE1 A:HIS96 3.0 4.0 1.0 CG A:HIS119 3.2 10.9 1.0 CE1 A:HIS94 3.4 8.0 1.0 CB A:HIS119 3.6 10.0 1.0 CG A:HIS94 4.0 12.6 1.0 C1 A:AZM400 4.0 24.2 1.0 O2 A:AZM400 4.0 23.4 1.0 OG1 A:THR199 4.1 24.1 1.0 NE2 A:HIS119 4.1 10.8 1.0 CG A:HIS96 4.2 2.0 1.0 ND1 A:HIS96 4.2 2.0 1.0 CD2 A:HIS119 4.2 9.9 1.0 CE2 A:PHE65 4.3 12.1 1.0 ND1 A:HIS94 4.3 7.8 1.0 OE1 A:GLU106 4.4 29.5 1.0 CZ A:PHE65 4.8 14.2 1.0 N3 A:AZM400 4.9 23.2 1.0 CD A:GLU106 5.0 24.9 1.0

Zinc binding site 2 out of 2 in the Complex Between Murine Mitochondrial Carbonic Anyhdrase V and the Transition State Analogue Acetazolamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Complex Between Murine Mitochondrial Carbonic Anyhdrase V and the Transition State Analogue Acetazolamide within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn280 b:23.0 occ:1.00 N1 B:AZM900 1.8 11.8 1.0 NE2 B:HIS96 2.0 2.0 1.0 ND1 B:HIS119 2.0 8.4 1.0 NE2 B:HIS94 2.2 12.6 1.0 CD2 B:HIS94 2.7 12.8 1.0 CE1 B:HIS119 2.8 11.1 1.0 CD2 B:HIS96 2.9 2.0 1.0 S1 B:AZM900 3.0 23.5 1.0 CE1 B:HIS96 3.1 2.0 1.0 CG B:HIS119 3.2 13.4 1.0 CE1 B:HIS94 3.4 16.3 1.0 CB B:HIS119 3.6 12.4 1.0 O1 B:AZM900 3.6 24.4 1.0 CG B:HIS94 4.0 20.0 1.0 NE2 B:HIS119 4.0 9.1 1.0 OG1 B:THR199 4.1 22.2 1.0 O2 B:AZM900 4.1 18.2 1.0 C1 B:AZM900 4.1 18.8 1.0 CG B:HIS96 4.1 2.0 1.0 OE1 B:GLU106 4.2 15.0 1.0 ND1 B:HIS96 4.2 2.6 1.0 CD2 B:HIS119 4.2 15.1 1.0 CE2 B:PHE65 4.3 9.7 1.0 ND1 B:HIS94 4.3 22.0 1.0 N3 B:AZM900 4.7 18.2 1.0 CZ B:PHE65 4.8 13.7 1.0 CD B:GLU106 5.0 12.5 1.0

P.A.Boriack-Sjodin, R.W.Heck, P.J.Laipis, D.N.Silverman, D.W.Christianson. Structure Determination of Murine Mitochondrial Carbonic Anhydrase V at 2.45-A Resolution: Implications For Catalytic Proton Transfer and Inhibitor Design. Proc.Natl.Acad.Sci.Usa V. 92 10949 1995.
ISSN: ISSN 0027-8424
PubMed: 7479916
DOI: 10.1073/PNAS.92.24.10949