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Zinc in PDB 1cvc: Redesigning the Zinc Binding Site of Human Carbonic Anhydrase II: Structure of A HIS2ASP-ZN2+ Metal Coordination Polyhedron

Enzymatic activity of Redesigning the Zinc Binding Site of Human Carbonic Anhydrase II: Structure of A HIS2ASP-ZN2+ Metal Coordination Polyhedron

All present enzymatic activity of Redesigning the Zinc Binding Site of Human Carbonic Anhydrase II: Structure of A HIS2ASP-ZN2+ Metal Coordination Polyhedron:
4.2.1.1;

Protein crystallography data

The structure of Redesigning the Zinc Binding Site of Human Carbonic Anhydrase II: Structure of A HIS2ASP-ZN2+ Metal Coordination Polyhedron, PDB code: 1cvc was solved by J.A.Ippolito, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.30
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 (%) n/a / n/a

Zinc Binding Sites:

The binding sites of Zinc atom in the Redesigning the Zinc Binding Site of Human Carbonic Anhydrase II: Structure of A HIS2ASP-ZN2+ Metal Coordination Polyhedron (pdb code 1cvc). 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 Redesigning the Zinc Binding Site of Human Carbonic Anhydrase II: Structure of A HIS2ASP-ZN2+ Metal Coordination Polyhedron, PDB code: 1cvc:

Zinc binding site 1 out of 1 in 1cvc

Go back to Zinc Binding Sites List in 1cvc
Zinc binding site 1 out of 1 in the Redesigning the Zinc Binding Site of Human Carbonic Anhydrase II: Structure of A HIS2ASP-ZN2+ Metal Coordination Polyhedron


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Redesigning the Zinc Binding Site of Human Carbonic Anhydrase II: Structure of A HIS2ASP-ZN2+ Metal Coordination Polyhedron within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:13.1
occ:1.00
 OD2 A:ASP94 2.1 11.7 1.0
ND1 A:HIS119 2.2 7.7 1.0
NE2 A:HIS96 2.4 8.3 1.0
O A:HOH348 2.4 24.9 1.0
O A:HOH351 2.6 19.2 1.0
CD2 A:HIS96 3.0 8.4 1.0
CG A:ASP94 3.1 12.0 1.0
CE1 A:HIS119 3.1 7.9 1.0
CG A:HIS119 3.2 8.0 1.0
OD1 A:ASP94 3.4 12.2 1.0
CE1 A:HIS96 3.5 8.5 1.0
CB A:HIS119 3.6 7.9 1.0
O A:HOH341 3.8 16.2 1.0
O A:HOH349 4.0 16.3 1.0
OE1 A:GLU106 4.2 7.8 1.0
CG A:HIS96 4.2 8.6 1.0
NE2 A:HIS119 4.3 8.0 1.0
CD2 A:HIS119 4.3 7.8 1.0
OG1 A:THR199 4.4 5.1 1.0
CB A:ASP94 4.4 11.7 1.0
ND1 A:HIS96 4.5 8.6 1.0
O A:ASP94 4.8 11.5 1.0
C A:ASP94 4.8 11.3 1.0
CA A:HIS119 4.9 8.1 1.0

Reference:

L.L.Kiefer, J.A.Ippolito, C.A.Fierke, D.W.Christianson. Redesigning the Zinc-Binding Site of Human Carbonic Anhydrase-II - Structure of A HIS2ASP-ZN2+ Metal Coordination Polyhedron. J.Am.Chem.Soc. V. 115 12581 1993.
ISSN: ISSN 0002-7863
Page generated: Mon Jan 25 16:08:07 2021

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