Atomistry » Zinc » PDB 3p3e-3pe8 » 3p44
Atomistry »
  Zinc »
    PDB 3p3e-3pe8 »
      3p44 »

Zinc in PDB 3p44: Human Carbonic Anhydrase II in Complex with P-(4-Ruthenocenyl-1H-1,2, 3-Triazol-1-Yl)Benzenesulfonamide

Enzymatic activity of Human Carbonic Anhydrase II in Complex with P-(4-Ruthenocenyl-1H-1,2, 3-Triazol-1-Yl)Benzenesulfonamide

All present enzymatic activity of Human Carbonic Anhydrase II in Complex with P-(4-Ruthenocenyl-1H-1,2, 3-Triazol-1-Yl)Benzenesulfonamide:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II in Complex with P-(4-Ruthenocenyl-1H-1,2, 3-Triazol-1-Yl)Benzenesulfonamide, PDB code: 3p44 was solved by A.J.Salmon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 24.73 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.500, 41.590, 72.290, 90.00, 104.64, 90.00
R / Rfree (%) 18.3 / 23.3

Other elements in 3p44:

The structure of Human Carbonic Anhydrase II in Complex with P-(4-Ruthenocenyl-1H-1,2, 3-Triazol-1-Yl)Benzenesulfonamide also contains other interesting chemical elements:

Ruthenium (Ru) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Carbonic Anhydrase II in Complex with P-(4-Ruthenocenyl-1H-1,2, 3-Triazol-1-Yl)Benzenesulfonamide (pdb code 3p44). 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 Human Carbonic Anhydrase II in Complex with P-(4-Ruthenocenyl-1H-1,2, 3-Triazol-1-Yl)Benzenesulfonamide, PDB code: 3p44:

Zinc binding site 1 out of 1 in 3p44

Go back to Zinc Binding Sites List in 3p44
Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II in Complex with P-(4-Ruthenocenyl-1H-1,2, 3-Triazol-1-Yl)Benzenesulfonamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Carbonic Anhydrase II in Complex with P-(4-Ruthenocenyl-1H-1,2, 3-Triazol-1-Yl)Benzenesulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn261

b:14.9
occ:1.00
NAK A:067300 2.1 14.9 1.0
NE2 A:HIS96 2.1 11.5 1.0
ND1 A:HIS119 2.1 10.3 1.0
NE2 A:HIS94 2.2 14.5 1.0
CD2 A:HIS96 2.9 10.3 1.0
CD2 A:HIS94 3.0 10.3 1.0
CE1 A:HIS119 3.0 10.5 1.0
CG A:HIS119 3.2 12.4 1.0
OAE A:067300 3.2 16.8 1.0
SAJ A:067300 3.2 14.9 1.0
CE1 A:HIS96 3.2 10.3 1.0
CE1 A:HIS94 3.3 12.3 1.0
CB A:HIS119 3.6 10.3 1.0
OG1 A:THR198 3.8 14.1 1.0
OE1 A:GLU106 3.9 17.3 1.0
CG A:HIS96 4.1 15.6 1.0
NE2 A:HIS119 4.2 10.3 1.0
CG A:HIS94 4.2 15.8 1.0
CAI A:067300 4.2 16.9 1.0
ND1 A:HIS96 4.2 13.9 1.0
CD2 A:HIS119 4.3 10.3 1.0
ND1 A:HIS94 4.3 10.3 1.0
OAO A:067300 4.3 15.2 1.0
C1 A:GOL301 4.4 23.2 1.0
CD A:GLU106 4.8 18.8 1.0
CAD A:067300 4.8 22.8 1.0
CAN A:067300 5.0 17.3 1.0

Reference:

A.J.Salmon, M.L.Williams, A.Hofmann, S.A.Poulsen. Protein Crystal Structures with Ferrocene and Ruthenocene-Based Enzyme Inhibitors. Chem.Commun.(Camb.) V. 48 2328 2012.
ISSN: ISSN 1359-7345
PubMed: 22258283
DOI: 10.1039/C2CC15625C
Page generated: Wed Dec 16 04:42:23 2020

Last articles

Zn in 7RRP
Zn in 7OKY
Zn in 7OL0
Zn in 7OKX
Zn in 7ONB
Zn in 7RSF
Zn in 7OUF
Zn in 7OUG
Zn in 7OUH
Zn in 7RGN
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy