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Zinc in PDB 4lu3: The Crystal Structure of the Human Carbonic Anhydrase Xiv

Enzymatic activity of The Crystal Structure of the Human Carbonic Anhydrase Xiv

All present enzymatic activity of The Crystal Structure of the Human Carbonic Anhydrase Xiv:
4.2.1.1;

Protein crystallography data

The structure of The Crystal Structure of the Human Carbonic Anhydrase Xiv, PDB code: 4lu3 was solved by V.Alterio, G.De Simone, S.M.Monti, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.00
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 88.610, 88.610, 108.900, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 20.6

Zinc Binding Sites:

The binding sites of Zinc atom in the The Crystal Structure of the Human Carbonic Anhydrase Xiv (pdb code 4lu3). 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 The Crystal Structure of the Human Carbonic Anhydrase Xiv, PDB code: 4lu3:

Zinc binding site 1 out of 1 in 4lu3

Go back to Zinc Binding Sites List in 4lu3
Zinc binding site 1 out of 1 in the The Crystal Structure of the Human Carbonic Anhydrase Xiv


Mono view


Stereo pair view

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

b:11.7
occ:1.00
NE2 A:HIS96 2.0 9.6 1.0
NE2 A:HIS94 2.0 9.7 1.0
N1 A:AZM302 2.0 12.3 1.0
ND1 A:HIS119 2.0 7.5 1.0
O2 A:AZM302 2.9 10.6 1.0
CD2 A:HIS94 3.0 7.7 1.0
CE1 A:HIS94 3.0 9.7 1.0
CE1 A:HIS119 3.0 6.8 1.0
S1 A:AZM302 3.0 12.3 1.0
CD2 A:HIS96 3.0 7.6 1.0
CE1 A:HIS96 3.0 8.9 1.0
CG A:HIS119 3.1 6.8 1.0
CB A:HIS119 3.5 8.1 1.0
OE1 A:GLU106 3.9 9.1 1.0
OG1 A:THR199 4.0 8.8 1.0
O1 A:AZM302 4.1 10.7 1.0
ND1 A:HIS94 4.1 7.4 1.0
CG A:HIS94 4.1 9.2 1.0
ND1 A:HIS96 4.1 7.8 1.0
CG A:HIS96 4.2 9.6 1.0
NE2 A:HIS119 4.2 7.3 1.0
C1 A:AZM302 4.2 14.6 1.0
CD2 A:HIS119 4.2 6.3 1.0
O1 A:GOL306 4.6 41.8 1.0
N3 A:AZM302 4.8 15.3 1.0
CD A:GLU106 4.9 12.7 1.0
C3 A:GOL306 4.9 37.6 1.0

Reference:

V.Alterio, P.Pan, S.Parkkila, M.Buonanno, C.T.Supuran, S.M.Monti, G.De Simone. The Structural Comparison Between Membrane-Associated Human Carbonic Anhydrases Provides Insights Into Drug Design of Selective Inhibitors. Biopolymers V. 101 769 2014.
ISSN: ISSN 0006-3525
PubMed: 24374484
DOI: 10.1002/BIP.22456
Page generated: Wed Dec 16 05:33:45 2020

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