Atomistry » Zinc » PDB 3e2d-3eb5 » 3e2w
Atomistry »
  Zinc »
    PDB 3e2d-3eb5 »
      3e2w »

Zinc in PDB 3e2w: H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate

Enzymatic activity of H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate

All present enzymatic activity of H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate:
4.2.1.1;

Protein crystallography data

The structure of H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate, PDB code: 3e2w was solved by R.S.Rowlett, J.Lee, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.20 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 250.141, 145.225, 53.499, 90.00, 93.78, 90.00
R / Rfree (%) 20.5 / 24.2

Zinc Binding Sites:

The binding sites of Zinc atom in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate (pdb code 3e2w). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate, PDB code: 3e2w:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 3e2w

Go back to Zinc Binding Sites List in 3e2w
Zinc binding site 1 out of 6 in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn230

b:67.5
occ:1.00
 OD1 A:ASP44 2.0 70.0 1.0
NE2 A:HIS98 2.1 65.9 1.0
SG A:CYS101 2.3 65.5 1.0
SG A:CYS42 2.3 65.8 1.0
CG A:ASP44 2.9 69.8 1.0
CE1 A:HIS98 2.9 65.0 1.0
OD2 A:ASP44 3.1 70.9 1.0
CD2 A:HIS98 3.2 65.6 1.0
CB A:CYS101 3.4 66.7 1.0
CB A:CYS42 3.4 66.0 1.0
CA A:CYS101 3.7 66.9 1.0
N A:GLY102 4.0 66.8 1.0
ND1 A:HIS98 4.1 63.4 1.0
O A:HOH243 4.2 54.7 1.0
C A:CYS101 4.2 66.8 1.0
CB A:ASP44 4.2 69.5 1.0
CG A:HIS98 4.2 64.6 1.0
N A:GLY103 4.4 67.4 1.0
N A:SER45 4.4 71.8 1.0
C A:ASP44 4.4 70.6 1.0
CA A:ASP44 4.6 69.8 1.0
N A:ASP44 4.7 69.2 1.0
CA A:ALA67 4.8 64.5 1.0
N A:ALA67 4.8 64.3 1.0
CA A:CYS42 4.8 66.3 1.0
O A:ASP44 4.9 70.6 1.0
OD1 A:ASN68 4.9 64.9 1.0

Zinc binding site 2 out of 6 in 3e2w

Go back to Zinc Binding Sites List in 3e2w
Zinc binding site 2 out of 6 in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn230

b:65.0
occ:1.00
 OD2 B:ASP44 2.0 67.8 1.0
NE2 B:HIS98 2.1 63.5 1.0
SG B:CYS42 2.3 64.8 1.0
SG B:CYS101 2.5 65.0 1.0
CE1 B:HIS98 2.9 63.4 1.0
CG B:ASP44 2.9 67.9 1.0
CD2 B:HIS98 3.2 64.5 1.0
CB B:ASP44 3.3 68.9 1.0
CB B:CYS42 3.4 64.3 1.0
CB B:CYS101 3.5 65.6 1.0
CA B:CYS101 3.8 66.0 1.0
OD1 B:ASP44 3.9 70.3 1.0
N B:GLY102 4.0 65.8 1.0
ND1 B:HIS98 4.0 62.8 1.0
CG B:HIS98 4.2 64.8 1.0
C B:CYS101 4.3 66.0 1.0
O B:HOH232 4.3 45.5 1.0
N B:GLY103 4.5 65.5 1.0
CA B:ASP44 4.5 68.5 1.0
N B:ASP44 4.6 67.6 1.0
N B:SER45 4.7 71.7 1.0
CA B:CYS42 4.8 64.4 1.0
N B:ALA67 4.9 61.7 1.0
CA B:ALA67 4.9 61.9 1.0
OD1 B:ASN68 5.0 58.7 1.0

Zinc binding site 3 out of 6 in 3e2w

Go back to Zinc Binding Sites List in 3e2w
Zinc binding site 3 out of 6 in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn230

b:66.8
occ:1.00
 OD2 C:ASP44 2.0 71.2 1.0
NE2 C:HIS98 2.1 66.6 1.0
SG C:CYS42 2.3 64.3 1.0
SG C:CYS101 2.3 67.1 1.0
CG C:ASP44 2.8 70.5 1.0
CE1 C:HIS98 2.9 65.1 1.0
CB C:ASP44 3.1 70.3 1.0
CD2 C:HIS98 3.2 65.1 1.0
CB C:CYS101 3.3 67.1 1.0
CB C:CYS42 3.3 64.6 1.0
CA C:CYS101 3.6 67.2 1.0
OD1 C:ASP44 3.9 74.6 1.0
ND1 C:HIS98 4.0 65.6 1.0
N C:GLY102 4.1 67.4 1.0
C C:CYS101 4.2 67.5 1.0
CG C:HIS98 4.2 64.9 1.0
CA C:ASP44 4.2 70.0 1.0
N C:ASP44 4.2 68.7 1.0
O C:HOH234 4.4 44.7 1.0
CA C:CYS42 4.7 65.0 1.0
N C:GLY103 4.7 68.2 1.0
C C:ASP44 4.9 70.9 1.0
N C:CYS101 4.9 67.3 1.0
N C:SER45 4.9 71.0 1.0
N C:ALA67 4.9 63.9 1.0

Zinc binding site 4 out of 6 in 3e2w

Go back to Zinc Binding Sites List in 3e2w
Zinc binding site 4 out of 6 in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn230

b:66.5
occ:1.00
 OD2 D:ASP44 2.0 64.5 1.0
NE2 D:HIS98 2.1 65.5 1.0
SG D:CYS101 2.3 65.0 1.0
SG D:CYS42 2.3 61.2 1.0
CG D:ASP44 2.8 64.3 1.0
CE1 D:HIS98 2.9 65.9 1.0
OD1 D:ASP44 3.1 65.8 1.0
CD2 D:HIS98 3.3 64.7 1.0
CB D:CYS42 3.3 61.6 1.0
CB D:CYS101 3.3 66.3 1.0
CA D:CYS101 3.7 66.2 1.0
N D:GLY102 4.0 66.5 1.0
C D:ASP44 4.0 64.3 1.0
CB D:ASP44 4.1 63.9 1.0
ND1 D:HIS98 4.1 64.9 1.0
N D:SER45 4.1 65.1 1.0
C D:CYS101 4.2 66.4 1.0
CA D:ASP44 4.3 63.6 1.0
CG D:HIS98 4.3 64.6 1.0
O D:HOH238 4.3 51.4 1.0
N D:ASP44 4.3 63.1 1.0
O D:ASP44 4.4 64.6 1.0
N D:GLY103 4.4 66.2 1.0
CA D:CYS42 4.7 61.4 1.0
CA D:SER45 4.9 65.2 1.0
C D:CYS42 5.0 61.5 1.0

Zinc binding site 5 out of 6 in 3e2w

Go back to Zinc Binding Sites List in 3e2w
Zinc binding site 5 out of 6 in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn230

b:64.5
occ:1.00
 OD2 E:ASP44 2.0 62.5 1.0
NE2 E:HIS98 2.1 62.9 1.0
SG E:CYS101 2.3 64.8 1.0
SG E:CYS42 2.3 61.7 1.0
CG E:ASP44 2.7 64.9 1.0
OD1 E:ASP44 2.8 66.6 1.0
CE1 E:HIS98 2.8 63.2 1.0
CD2 E:HIS98 3.3 62.8 1.0
CB E:CYS42 3.3 61.6 1.0
CB E:CYS101 3.3 64.3 1.0
CA E:CYS101 3.8 64.4 1.0
ND1 E:HIS98 4.0 62.6 1.0
CB E:ASP44 4.0 65.0 1.0
N E:GLY102 4.1 64.4 1.0
C E:CYS101 4.2 64.3 1.0
O E:HOH254 4.2 51.4 1.0
CG E:HIS98 4.3 63.1 1.0
C E:ASP44 4.3 66.4 1.0
N E:GLY103 4.4 64.5 1.0
CA E:ASP44 4.4 65.5 1.0
N E:ASP44 4.4 64.5 1.0
N E:SER45 4.4 67.7 1.0
O E:ASP44 4.6 65.9 1.0
CA E:CYS42 4.7 61.9 1.0
OD1 E:ASN68 5.0 60.7 1.0
O E:CYS101 5.0 64.2 1.0

Zinc binding site 6 out of 6 in 3e2w

Go back to Zinc Binding Sites List in 3e2w
Zinc binding site 6 out of 6 in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 1M Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Zn230

b:68.4
occ:1.00
 OD2 F:ASP44 2.0 70.1 1.0
NE2 F:HIS98 2.1 66.1 1.0
SG F:CYS42 2.3 65.2 1.0
SG F:CYS101 2.3 64.5 1.0
CG F:ASP44 2.8 70.0 1.0
OD1 F:ASP44 2.9 73.0 1.0
CE1 F:HIS98 3.0 65.4 1.0
CD2 F:HIS98 3.1 65.3 1.0
CB F:CYS101 3.3 66.1 1.0
CB F:CYS42 3.3 65.4 1.0
CA F:CYS101 3.6 66.1 1.0
ND1 F:HIS98 4.1 64.3 1.0
N F:GLY102 4.2 66.2 1.0
CB F:ASP44 4.2 70.3 1.0
CG F:HIS98 4.2 65.0 1.0
C F:CYS101 4.2 66.1 1.0
O F:HOH237 4.4 47.6 1.0
N F:ASP44 4.5 69.0 1.0
N F:GLY103 4.6 66.8 1.0
CA F:ASP44 4.6 70.1 1.0
C F:ASP44 4.6 71.2 1.0
CA F:CYS42 4.7 65.5 1.0
N F:SER45 4.8 72.2 1.0
N F:CYS101 4.9 66.1 1.0
N F:ALA67 4.9 63.1 1.0
O F:ASP44 5.0 71.8 1.0

Reference:

R.S.Rowlett, C.Tu, J.Lee, A.G.Herman, D.A.Chapnick, S.H.Shah, P.C.Gareiss. Allosteric Site Variants of Haemophilus Influenzae Beta-Carbonic Anhydrase. Biochemistry V. 48 6146 2009.
ISSN: ISSN 0006-2960
PubMed: 19459702
DOI: 10.1021/BI900663H
Page generated: Thu Oct 24 12:33:39 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