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Zinc in PDB 3e2a: H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 100 Mm Bicarbonate

Enzymatic activity of H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 100 Mm Bicarbonate

All present enzymatic activity of H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 100 Mm Bicarbonate:
4.2.1.1;

Protein crystallography data

The structure of H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 100 Mm Bicarbonate, PDB code: 3e2a 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) 24.78 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 230.606, 145.512, 53.234, 90.00, 93.78, 90.00
R / Rfree (%) 20.1 / 24.4

Zinc Binding Sites:

The binding sites of Zinc atom in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 100 Mm Bicarbonate (pdb code 3e2a). 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 100 Mm Bicarbonate, PDB code: 3e2a:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 3e2a

Go back to Zinc Binding Sites List in 3e2a
Zinc binding site 1 out of 6 in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 100 Mm 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 100 Mm Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn230

b:48.8
occ:1.00
 OD2 A:ASP44 2.0 57.2 1.0
NE2 A:HIS98 2.1 49.7 1.0
SG A:CYS101 2.3 44.8 1.0
SG A:CYS42 2.3 45.5 1.0
CE1 A:HIS98 2.8 47.2 1.0
CG A:ASP44 3.0 54.0 1.0
CD2 A:HIS98 3.2 48.0 1.0
CB A:ASP44 3.2 52.7 1.0
CB A:CYS101 3.3 44.9 1.0
CB A:CYS42 3.3 45.7 1.0
CA A:CYS101 3.6 44.9 1.0
ND1 A:HIS98 4.0 47.0 1.0
N A:GLY102 4.0 44.7 1.0
N A:SER45 4.0 53.8 1.0
O A:HOH253 4.1 35.6 1.0
C A:CYS101 4.1 44.6 1.0
OD1 A:ASP44 4.2 58.2 1.0
CG A:HIS98 4.2 46.6 1.0
CA A:ASP44 4.2 51.9 1.0
N A:ASP44 4.3 50.8 1.0
N A:GLY103 4.3 45.5 1.0
C A:ASP44 4.6 53.3 1.0
CA A:CYS42 4.7 45.8 1.0
N A:ALA67 4.8 39.8 1.0
N A:CYS101 4.8 45.6 1.0
CA A:SER45 4.9 53.5 1.0
CA A:ALA67 4.9 39.7 1.0
C A:CYS42 4.9 46.8 1.0
OD1 A:ASN68 5.0 43.9 1.0
CA A:GLY102 5.0 44.8 1.0
CA A:GLY103 5.0 45.5 1.0

Zinc binding site 2 out of 6 in 3e2a

Go back to Zinc Binding Sites List in 3e2a
Zinc binding site 2 out of 6 in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 100 Mm 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 100 Mm Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn230

b:42.9
occ:1.00
 OD2 B:ASP44 2.0 52.3 1.0
NE2 B:HIS98 2.1 39.5 1.0
SG B:CYS42 2.3 42.1 1.0
SG B:CYS101 2.3 41.5 1.0
CG B:ASP44 3.0 50.0 1.0
CE1 B:HIS98 3.0 37.8 1.0
CD2 B:HIS98 3.1 38.5 1.0
CB B:CYS42 3.3 42.9 1.0
CB B:ASP44 3.3 48.2 1.0
CB B:CYS101 3.3 42.1 1.0
CA B:CYS101 3.6 42.5 1.0
N B:GLY102 3.9 41.9 1.0
CA B:ASP44 4.0 47.8 1.0
N B:ASP44 4.1 47.2 1.0
C B:CYS101 4.1 42.3 1.0
OD1 B:ASP44 4.1 57.6 1.0
ND1 B:HIS98 4.1 37.3 1.0
N B:SER45 4.2 48.6 1.0
C B:ASP44 4.2 48.0 1.0
CG B:HIS98 4.2 40.6 1.0
O B:HOH236 4.2 28.9 1.0
N B:GLY103 4.4 42.1 1.0
CA B:CYS42 4.7 43.1 1.0
O B:ASP44 4.7 48.3 1.0
N B:ALA67 4.8 41.5 1.0
N B:CYS101 4.9 42.7 1.0
C B:CYS42 4.9 43.4 1.0
CA B:ALA67 4.9 42.1 1.0

Zinc binding site 3 out of 6 in 3e2a

Go back to Zinc Binding Sites List in 3e2a
Zinc binding site 3 out of 6 in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 100 Mm 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 100 Mm Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn230

b:42.6
occ:1.00
 OD2 C:ASP44 2.0 42.7 1.0
NE2 C:HIS98 2.1 41.3 1.0
SG C:CYS42 2.3 39.4 1.0
SG C:CYS101 2.3 42.0 1.0
CG C:ASP44 2.9 44.1 1.0
CE1 C:HIS98 2.9 41.5 1.0
CD2 C:HIS98 3.1 40.8 1.0
OD1 C:ASP44 3.1 45.3 1.0
CB C:CYS101 3.3 42.0 1.0
CB C:CYS42 3.3 40.6 1.0
CA C:CYS101 3.6 42.0 1.0
ND1 C:HIS98 4.0 41.7 1.0
N C:GLY102 4.0 41.6 1.0
C C:CYS101 4.1 41.8 1.0
CG C:HIS98 4.2 41.2 1.0
C C:ASP44 4.2 45.8 1.0
CB C:ASP44 4.2 44.8 1.0
O C:HOH235 4.2 27.4 1.0
N C:SER45 4.2 46.4 1.0
N C:GLY103 4.3 41.5 1.0
N C:ASP44 4.4 43.7 1.0
O C:ASP44 4.4 46.8 1.0
CA C:ASP44 4.5 44.8 1.0
CA C:CYS42 4.7 40.7 1.0
N C:ALA67 4.8 39.5 1.0
CA C:ALA67 4.8 39.5 1.0
N C:CYS101 4.9 42.4 1.0
OD1 C:ASN68 4.9 40.3 1.0
O C:CYS101 4.9 41.6 1.0
CA C:SER45 5.0 47.3 1.0
CA C:GLY103 5.0 41.9 1.0

Zinc binding site 4 out of 6 in 3e2a

Go back to Zinc Binding Sites List in 3e2a
Zinc binding site 4 out of 6 in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 100 Mm 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 100 Mm Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn230

b:41.8
occ:1.00
 OD1 D:ASP44 2.0 44.4 1.0
NE2 D:HIS98 2.1 41.6 1.0
SG D:CYS101 2.3 40.1 1.0
SG D:CYS42 2.3 38.4 1.0
CG D:ASP44 3.0 46.6 1.0
CD2 D:HIS98 3.0 41.0 1.0
CE1 D:HIS98 3.1 39.9 1.0
CB D:CYS42 3.2 39.2 1.0
CB D:CYS101 3.4 40.9 1.0
CB D:ASP44 3.4 46.7 1.0
CA D:CYS101 3.7 40.7 1.0
N D:GLY102 4.0 40.0 1.0
OD2 D:ASP44 4.1 48.3 1.0
C D:CYS101 4.2 40.4 1.0
CG D:HIS98 4.2 40.6 1.0
ND1 D:HIS98 4.2 40.5 1.0
N D:ASP44 4.2 44.8 1.0
O D:HOH238 4.3 32.3 1.0
N D:SER45 4.3 47.9 1.0
CA D:ASP44 4.3 45.8 1.0
N D:GLY103 4.3 39.9 1.0
CA D:CYS42 4.6 39.0 1.0
N D:ALA67 4.8 39.1 1.0
CA D:ALA67 4.8 38.8 1.0
C D:ASP44 4.9 47.4 1.0
C D:CYS42 4.9 39.5 1.0
OD1 D:ASN68 5.0 39.4 1.0
CA D:GLY102 5.0 39.9 1.0
N D:CYS101 5.0 41.1 1.0

Zinc binding site 5 out of 6 in 3e2a

Go back to Zinc Binding Sites List in 3e2a
Zinc binding site 5 out of 6 in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 100 Mm 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 100 Mm Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn230

b:41.9
occ:1.00
 OD2 E:ASP44 2.0 40.9 1.0
NE2 E:HIS98 2.1 38.0 1.0
SG E:CYS42 2.3 39.4 1.0
SG E:CYS101 2.3 38.7 1.0
CG E:ASP44 2.8 42.1 1.0
CE1 E:HIS98 2.9 38.5 1.0
OD1 E:ASP44 3.1 44.3 1.0
CD2 E:HIS98 3.1 38.1 1.0
CB E:CYS42 3.2 38.0 1.0
CB E:CYS101 3.3 39.5 1.0
CA E:CYS101 3.6 39.8 1.0
N E:GLY102 4.0 40.0 1.0
ND1 E:HIS98 4.1 39.8 1.0
C E:CYS101 4.1 39.8 1.0
CB E:ASP44 4.1 42.0 1.0
C E:ASP44 4.1 43.5 1.0
N E:SER45 4.2 45.0 1.0
O E:HOH249 4.2 35.9 1.0
CG E:HIS98 4.2 40.1 1.0
N E:GLY103 4.3 40.1 1.0
N E:ASP44 4.4 41.5 1.0
CA E:ASP44 4.4 42.4 1.0
O E:ASP44 4.5 43.6 1.0
CA E:CYS42 4.6 38.5 1.0
N E:ALA67 4.8 38.8 1.0
OD1 E:ASN68 4.9 39.6 1.0
CA E:ALA67 4.9 38.5 1.0
N E:CYS101 4.9 39.9 1.0
CA E:SER45 5.0 45.9 1.0
C E:CYS42 5.0 38.5 1.0

Zinc binding site 6 out of 6 in 3e2a

Go back to Zinc Binding Sites List in 3e2a
Zinc binding site 6 out of 6 in the H. Influenzae Beta-Carbonic Anhydrase, Variant Y181F with 100 Mm 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 100 Mm Bicarbonate within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Zn230

b:44.3
occ:1.00
 OD1 F:ASP44 2.0 53.7 1.0
NE2 F:HIS98 2.1 41.5 1.0
SG F:CYS101 2.3 39.4 1.0
SG F:CYS42 2.3 39.1 1.0
CG F:ASP44 2.8 49.1 1.0
CE1 F:HIS98 2.9 40.2 1.0
CB F:ASP44 3.0 48.4 1.0
CD2 F:HIS98 3.1 41.2 1.0
CB F:CYS42 3.2 40.4 1.0
CB F:CYS101 3.3 40.5 1.0
CA F:CYS101 3.6 40.2 1.0
OD2 F:ASP44 3.9 56.1 1.0
N F:GLY102 4.0 40.5 1.0
ND1 F:HIS98 4.1 38.9 1.0
CA F:ASP44 4.1 47.8 1.0
N F:ASP44 4.2 46.3 1.0
CG F:HIS98 4.2 40.9 1.0
C F:CYS101 4.2 40.4 1.0
O F:HOH237 4.4 30.3 1.0
N F:GLY103 4.5 41.4 1.0
N F:SER45 4.5 50.1 1.0
C F:ASP44 4.5 49.0 1.0
CA F:CYS42 4.6 40.7 1.0
N F:ALA67 4.8 37.1 1.0
CA F:ALA67 4.8 37.6 1.0
N F:CYS101 4.9 40.0 1.0
C F:CYS42 4.9 41.2 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 12:31:09 2024

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