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Zinc in PDB 2esf: Identification of A Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial Beta-Carbonic Anhydrase

Enzymatic activity of Identification of A Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial Beta-Carbonic Anhydrase

All present enzymatic activity of Identification of A Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial Beta-Carbonic Anhydrase:
4.2.1.1;

Protein crystallography data

The structure of Identification of A Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial Beta-Carbonic Anhydrase, PDB code: 2esf was solved by J.D.Cronk, R.S.Rowlett, K.Y.J.Zhang, C.Tu, J.A.Endrizzi, P.C.Gareiss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.50 / 2.25
Space group P 43 2 2
Cell size a, b, c (Å), α, β, γ (°) 82.866, 82.866, 162.213, 90.00, 90.00, 90.00
R / Rfree (%) 19.8 / 22.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Identification of A Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial Beta-Carbonic Anhydrase (pdb code 2esf). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Identification of A Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial Beta-Carbonic Anhydrase, PDB code: 2esf:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2esf

Go back to Zinc Binding Sites List in 2esf
Zinc binding site 1 out of 2 in the Identification of A Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial Beta-Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Identification of A Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial Beta-Carbonic Anhydrase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn300

b:37.7
occ:1.00
NE2 A:HIS98 2.2 38.7 1.0
OD2 A:ASP44 2.3 43.6 1.0
SG A:CYS42 2.3 34.6 1.0
SG A:CYS101 2.3 34.4 1.0
CE1 A:HIS98 3.0 37.5 1.0
CG A:ASP44 3.1 44.9 1.0
CB A:CYS42 3.2 31.4 1.0
CD2 A:HIS98 3.2 40.6 1.0
CB A:CYS101 3.3 28.8 1.0
CB A:ASP44 3.4 37.1 1.0
CA A:CYS101 3.7 32.4 1.0
ND1 A:HIS98 4.1 38.5 1.0
N A:GLY102 4.2 33.9 1.0
OD1 A:ASP44 4.2 48.5 1.0
O A:HOH1504 4.2 29.1 1.0
CG A:HIS98 4.3 37.8 1.0
C A:CYS101 4.3 34.6 1.0
N A:ASP44 4.5 31.9 1.0
CA A:ASP44 4.6 32.2 1.0
O A:HOH1500 4.6 35.7 1.0
N A:GLY103 4.6 39.5 1.0
N A:ALA67 4.6 30.0 1.0
CA A:CYS42 4.6 35.0 1.0
CA A:ALA67 4.7 28.9 1.0
O A:HOH1572 4.8 49.9 1.0
N A:CYS101 5.0 37.6 1.0

Zinc binding site 2 out of 2 in 2esf

Go back to Zinc Binding Sites List in 2esf
Zinc binding site 2 out of 2 in the Identification of A Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial Beta-Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Identification of A Novel Non-Catalytic Bicarbonate Binding Site in Eubacterial Beta-Carbonic Anhydrase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn300

b:45.2
occ:1.00
OD2 B:ASP44 2.2 39.1 1.0
NE2 B:HIS98 2.3 48.3 1.0
SG B:CYS42 2.4 41.2 1.0
SG B:CYS101 2.5 48.6 1.0
CE1 B:HIS98 3.0 46.1 1.0
CG B:ASP44 3.1 40.5 1.0
CB B:CYS101 3.2 47.9 1.0
CB B:CYS42 3.3 35.8 1.0
CB B:ASP44 3.3 30.3 1.0
CD2 B:HIS98 3.4 48.8 1.0
CA B:CYS101 3.6 50.9 1.0
N B:GLY102 4.1 41.3 1.0
ND1 B:HIS98 4.2 45.5 1.0
C B:CYS101 4.2 50.8 1.0
OD1 B:ASP44 4.3 47.9 1.0
CG B:HIS98 4.4 44.5 1.0
N B:ASP44 4.4 38.0 1.0
O B:HOH2526 4.4 44.0 1.0
CA B:ASP44 4.5 33.8 1.0
N B:ALA67 4.6 42.5 1.0
O B:HOH2500 4.6 44.5 1.0
N B:GLY103 4.6 41.9 1.0
CA B:ALA67 4.7 39.0 1.0
CA B:CYS42 4.7 37.7 1.0
N B:CYS101 4.8 53.3 1.0
OD1 B:ASN68 5.0 46.7 1.0

Reference:

J.D.Cronk, R.S.Rowlett, K.Y.J.Zhang, C.Tu, J.A.Endrizzi, J.Lee, P.C.Gareiss, J.R.Preiss. Identification of A Novel Noncatalytic Bicarbonate Binding Site in Eubacterial Beta-Carbonic Anhydrase. Biochemistry V. 45 4351 2006.
ISSN: ISSN 0006-2960
PubMed: 16584170
DOI: 10.1021/BI052272Q
Page generated: Wed Dec 16 03:27:34 2020

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