Atomistry » Zinc » PDB 2vqx-2w13 » 2vun
Atomistry »
  Zinc »
    PDB 2vqx-2w13 »
      2vun »

Zinc in PDB 2vun: The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily

Enzymatic activity of The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily

All present enzymatic activity of The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily:
3.5.2.18;

Protein crystallography data

The structure of The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily, PDB code: 2vun was solved by D.Kress, A.Alhapel, A.J.Pierik, L.-O.Essen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 107.83 / 1.89
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 146.352, 159.824, 161.683, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 19.8

Other elements in 2vun:

The structure of The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily also contains other interesting chemical elements:

Iron (Fe) 4 atoms
Chlorine (Cl) 4 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily (pdb code 2vun). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily, PDB code: 2vun:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2vun

Go back to Zinc Binding Sites List in 2vun
Zinc binding site 1 out of 4 in the The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily


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 Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:26.9
occ:1.00
 OE2 A:GLU164 2.0 21.4 1.0
NE2 A:HIS69 2.1 20.0 1.0
NE2 A:HIS67 2.1 16.7 1.0
O A:HOH2362 2.1 31.3 1.0
OD1 A:ASP276 2.5 19.0 1.0
CE1 A:HIS69 2.9 19.4 1.0
CE1 A:HIS67 3.0 15.6 1.0
CD A:GLU164 3.0 19.5 1.0
CD2 A:HIS67 3.1 14.4 1.0
CL A:CL501 3.2 51.0 1.0
CD2 A:HIS69 3.2 18.3 1.0
CG A:ASP276 3.3 18.6 1.0
OE1 A:GLU164 3.5 21.8 1.0
FE A:FE402 3.6 25.3 1.0
OD2 A:ASP276 3.7 18.8 1.0
O A:HOH2205 3.9 30.1 1.0
ND1 A:HIS69 4.1 18.2 1.0
ND1 A:HIS67 4.1 14.4 1.0
CG A:HIS67 4.2 15.1 1.0
CG A:HIS69 4.3 16.4 1.0
CD2 A:HIS220 4.3 17.1 1.0
CG A:GLU164 4.3 19.0 1.0
CB A:ASP276 4.3 16.3 1.0
NE2 A:HIS220 4.5 18.8 1.0
CB A:ALA99 4.6 14.6 1.0
O A:HOH2222 4.7 28.3 1.0
CA A:ASP276 4.7 16.4 1.0
O A:HOH2275 4.8 48.3 1.0

Zinc binding site 2 out of 4 in 2vun

Go back to Zinc Binding Sites List in 2vun
Zinc binding site 2 out of 4 in the The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn401

b:31.4
occ:1.00
 OE2 B:GLU164 2.0 28.2 1.0
O B:HOH2314 2.0 34.0 1.0
OD1 B:ASP276 2.0 24.5 1.0
NE2 B:HIS67 2.1 21.9 1.0
NE2 B:HIS69 2.1 24.2 1.0
CE1 B:HIS69 2.9 22.3 1.0
CE1 B:HIS67 3.0 19.8 1.0
CD B:GLU164 3.0 26.1 1.0
CG B:ASP276 3.1 21.6 1.0
CD2 B:HIS67 3.1 19.7 1.0
CD2 B:HIS69 3.2 22.7 1.0
CL B:CL501 3.3 49.9 1.0
OE1 B:GLU164 3.5 29.1 1.0
OD2 B:ASP276 3.6 24.6 1.0
FE B:FE402 3.7 31.4 1.0
O B:HOH2173 3.9 36.8 1.0
O B:HOH2227 4.1 51.7 1.0
ND1 B:HIS69 4.1 22.0 1.0
ND1 B:HIS67 4.1 19.7 1.0
CD2 B:HIS220 4.2 21.4 1.0
CG B:HIS67 4.2 18.2 1.0
CB B:ASP276 4.2 19.5 1.0
CG B:HIS69 4.3 20.7 1.0
CG B:GLU164 4.3 26.6 1.0
NE2 B:HIS220 4.5 24.2 1.0
CB B:ALA99 4.6 18.9 1.0
O B:HOH2188 4.6 39.3 1.0
CA B:ASP276 4.7 19.2 1.0

Zinc binding site 3 out of 4 in 2vun

Go back to Zinc Binding Sites List in 2vun
Zinc binding site 3 out of 4 in the The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn401

b:33.7
occ:1.00
 OE2 C:GLU164 2.0 30.7 1.0
OD1 C:ASP276 2.0 26.2 1.0
NE2 C:HIS67 2.1 21.8 1.0
O C:HOH2312 2.1 34.0 1.0
NE2 C:HIS69 2.1 25.3 1.0
CE1 C:HIS69 3.0 23.2 1.0
CE1 C:HIS67 3.0 20.2 1.0
CG C:ASP276 3.0 23.2 1.0
CD C:GLU164 3.1 27.9 1.0
CD2 C:HIS67 3.1 19.4 1.0
CD2 C:HIS69 3.2 22.5 1.0
CL C:CL501 3.4 56.4 1.0
OE1 C:GLU164 3.6 30.7 1.0
OD2 C:ASP276 3.6 25.6 1.0
FE C:FE402 3.7 32.5 1.0
O C:HOH2177 3.9 37.7 1.0
O C:HOH2215 4.1 50.9 1.0
ND1 C:HIS67 4.1 19.2 1.0
ND1 C:HIS69 4.1 22.6 1.0
CB C:ASP276 4.2 21.2 1.0
CD2 C:HIS220 4.2 25.2 1.0
CG C:HIS67 4.2 17.6 1.0
CG C:HIS69 4.3 21.1 1.0
CG C:GLU164 4.3 27.7 1.0
NE2 C:HIS220 4.5 26.6 1.0
CA C:ASP276 4.6 20.9 1.0
CB C:ALA99 4.6 18.8 1.0
O C:HOH2186 4.7 41.9 1.0

Zinc binding site 4 out of 4 in 2vun

Go back to Zinc Binding Sites List in 2vun
Zinc binding site 4 out of 4 in the The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of The Crystal Structure of Enamidase at 1.9 A Resolution - A New Member of the Amidohydrolase Superfamily within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn401

b:33.2
occ:1.00
 OE2 D:GLU164 2.0 29.2 1.0
OD1 D:ASP276 2.0 25.3 1.0
O D:HOH2246 2.1 30.8 1.0
NE2 D:HIS67 2.1 22.2 1.0
NE2 D:HIS69 2.1 25.8 1.0
CE1 D:HIS69 2.9 24.6 1.0
CE1 D:HIS67 3.0 20.3 1.0
CG D:ASP276 3.0 22.4 1.0
CD D:GLU164 3.1 28.1 1.0
CD2 D:HIS67 3.1 19.7 1.0
CD2 D:HIS69 3.2 24.5 1.0
CL D:CL501 3.2 61.6 1.0
OE1 D:GLU164 3.5 31.5 1.0
OD2 D:ASP276 3.6 23.7 1.0
FE D:FE402 3.6 33.6 1.0
O D:HOH2139 3.7 37.0 1.0
ND1 D:HIS69 4.1 23.2 1.0
ND1 D:HIS67 4.1 19.7 1.0
CB D:ASP276 4.2 21.1 1.0
CG D:HIS67 4.2 19.2 1.0
CG D:HIS69 4.2 22.1 1.0
CD2 D:HIS220 4.3 22.9 1.0
CG D:GLU164 4.3 28.0 1.0
O D:HOH2149 4.6 38.8 1.0
CA D:ASP276 4.6 20.7 1.0
NE2 D:HIS220 4.6 25.1 1.0
CB D:ALA99 4.6 19.4 1.0
O D:HOH2150 4.6 47.7 1.0

Reference:

D.Kress, A.Alhapel, A.J.Pierik, L.-O.Essen. The Crystal Structure of Enamidase: A Bifunctional Enzyme of the Nicotinate Catabolism. J.Mol.Biol. V. 384 837 2008.
ISSN: ISSN 0022-2836
PubMed: 18805424
DOI: 10.1016/J.JMB.2008.09.002
Page generated: Thu Oct 17 04:34:12 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy