Atomistry » Zinc » PDB 4pog-4q1l » 4pyx
Atomistry »
  Zinc »
    PDB 4pog-4q1l »
      4pyx »

Zinc in PDB 4pyx: Crystal Structure of Human Carbonic Anhydrase Isozyme II with Inhibitor

Enzymatic activity of Crystal Structure of Human Carbonic Anhydrase Isozyme II with Inhibitor

All present enzymatic activity of Crystal Structure of Human Carbonic Anhydrase Isozyme II with Inhibitor:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of Human Carbonic Anhydrase Isozyme II with Inhibitor, PDB code: 4pyx was solved by A.Smirnov, E.Manakova, S.Grazulis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.22 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.022, 41.143, 71.519, 90.00, 104.07, 90.00
R / Rfree (%) 17.8 / 23

Other elements in 4pyx:

The structure of Crystal Structure of Human Carbonic Anhydrase Isozyme II with Inhibitor also contains other interesting chemical elements:

Fluorine (F) 3 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Carbonic Anhydrase Isozyme II with Inhibitor (pdb code 4pyx). 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 Crystal Structure of Human Carbonic Anhydrase Isozyme II with Inhibitor, PDB code: 4pyx:

Zinc binding site 1 out of 1 in 4pyx

Go back to Zinc Binding Sites List in 4pyx
Zinc binding site 1 out of 1 in the Crystal Structure of Human Carbonic Anhydrase Isozyme II with Inhibitor


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Human Carbonic Anhydrase Isozyme II with Inhibitor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:11.6
occ:1.00
NE2 A:HIS94 2.0 13.5 1.0
NE2 A:HIS96 2.0 8.8 1.0
N11 A:V90304 2.0 10.4 1.0
ND1 A:HIS119 2.1 8.5 1.0
CD2 A:HIS96 2.9 7.7 1.0
CD2 A:HIS94 2.9 12.6 1.0
CE1 A:HIS119 3.0 8.2 1.0
S8 A:V90304 3.0 11.9 1.0
CE1 A:HIS94 3.0 12.9 1.0
O10 A:V90304 3.1 10.1 1.0
CE1 A:HIS96 3.1 8.4 1.0
CG A:HIS119 3.1 7.9 1.0
CB A:HIS119 3.6 7.9 1.0
OE1 A:GLU106 3.7 9.6 1.0
C26 A:V90304 3.8 16.1 1.0
OG1 A:THR199 3.8 8.7 1.0
N7 A:V90304 4.0 14.5 1.0
CG A:HIS94 4.1 12.9 1.0
O9 A:V90304 4.1 10.6 1.0
NE2 A:HIS119 4.1 8.0 1.0
ND1 A:HIS94 4.1 13.5 1.0
CG A:HIS96 4.1 7.6 1.0
ND1 A:HIS96 4.2 8.0 1.0
CD2 A:HIS119 4.2 9.1 1.0
C3 A:V90304 4.3 13.5 1.0
C19 A:V90304 4.5 15.3 1.0
C4 A:V90304 4.6 13.9 1.0
CD A:GLU106 4.7 9.8 1.0
C20 A:V90304 4.8 16.0 1.0
CH2 A:TRP209 4.9 9.5 1.0

Reference:

V.Dudutiene, J.Matuliene, A.Smirnov, D.D.Timm, A.Zubriene, L.Baranauskiene, V.Morkunaite, J.Smirnoviene, V.Michailoviene, V.Juozapaitiene, A.Mickeviciute, J.Kazokaite, S.Baksyte, A.Kasiliauskaite, J.Jachno, J.Revuckiene, M.Kisonaite, V.Pilipuityte, E.Ivanauskaite, G.Milinaviciute, V.Smirnovas, V.Petrikaite, V.Kairys, V.Petrauskas, P.Norvaisas, D.Linge, P.Gibieza, E.Capkauskaite, A.Zaksauskas, E.Kazlauskas, E.Manakova, S.Grazulis, J.E.Ladbury, D.Matulis. Discovery and Characterization of Novel Selective Inhibitors of Carbonic Anhydrase IX. J.Med.Chem. V. 57 9435 2014.
ISSN: ISSN 0022-2623
PubMed: 25358084
DOI: 10.1021/JM501003K
Page generated: Sun Oct 27 06:10:28 2024

Last articles

Zn in 9FD2
Zn in 9GUW
Zn in 9GUX
Zn in 9F7C
Zn in 9GUR
Zn in 9F7A
Zn in 9DDE
Zn in 9DBY
Zn in 9EBZ
Zn in 9DGG
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy