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Zinc in PDB 2a8c: Haemophilus Influenzae Beta-Carbonic Anhydrase

Enzymatic activity of Haemophilus Influenzae Beta-Carbonic Anhydrase

All present enzymatic activity of Haemophilus Influenzae Beta-Carbonic Anhydrase:
4.2.1.1;

Protein crystallography data

The structure of Haemophilus Influenzae Beta-Carbonic Anhydrase, PDB code: 2a8c was solved by J.D.Cronk, R.S.Rowlett, K.Y.J.Zhang, C.Tu, J.A.Endrizzi, J.Lee, P.C.Gareiss, J.R.Preiss, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 2.30
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 232.655, 144.726, 52.408, 90.00, 93.97, 90.00
R / Rfree (%) 21.5 / 25.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Haemophilus Influenzae Beta-Carbonic Anhydrase (pdb code 2a8c). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 6 binding sites of Zinc where determined in the Haemophilus Influenzae Beta-Carbonic Anhydrase, PDB code: 2a8c:
Jump to Zinc binding site number: 1; 2; 3; 4; 5; 6;

Zinc binding site 1 out of 6 in 2a8c

Go back to Zinc Binding Sites List in 2a8c
Zinc binding site 1 out of 6 in the Haemophilus Influenzae 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 Haemophilus Influenzae Beta-Carbonic Anhydrase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1230

b:43.2
occ:1.00
OD2 A:ASP44 1.8 45.0 1.0
NE2 A:HIS98 1.9 45.4 1.0
SG A:CYS42 2.3 38.4 1.0
SG A:CYS101 2.3 43.0 1.0
CE1 A:HIS98 2.5 45.8 1.0
CG A:ASP44 2.7 46.1 1.0
CB A:ASP44 3.0 47.4 1.0
CD2 A:HIS98 3.1 42.9 1.0
CB A:CYS42 3.2 33.5 1.0
CB A:CYS101 3.3 43.2 1.0
CA A:CYS101 3.7 43.5 1.0
ND1 A:HIS98 3.8 45.6 1.0
OD1 A:ASP44 3.8 47.4 1.0
CG A:HIS98 4.0 43.3 1.0
N A:GLY102 4.2 40.5 1.0
CA A:ASP44 4.2 49.0 1.0
O A:HOH1233 4.2 32.2 1.0
N A:ASP44 4.2 42.9 1.0
C A:CYS101 4.3 42.2 1.0
N A:GLY103 4.4 40.4 1.0
CA A:CYS42 4.6 34.8 1.0
N A:ALA67 4.8 36.4 1.0
CA A:ALA67 4.8 35.2 1.0
C A:CYS42 5.0 34.5 1.0

Zinc binding site 2 out of 6 in 2a8c

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Zinc binding site 2 out of 6 in the Haemophilus Influenzae 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 Haemophilus Influenzae Beta-Carbonic Anhydrase within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn2230

b:44.6
occ:1.00
OD2 B:ASP44 1.9 39.8 1.0
NE2 B:HIS98 2.0 53.7 1.0
SG B:CYS101 2.2 38.4 1.0
SG B:CYS42 2.3 44.5 1.0
CG B:ASP44 2.8 44.6 1.0
CE1 B:HIS98 2.9 52.9 1.0
CD2 B:HIS98 3.0 51.4 1.0
CB B:ASP44 3.2 48.5 1.0
CB B:CYS101 3.2 42.3 1.0
CB B:CYS42 3.2 39.9 1.0
CA B:CYS101 3.6 44.6 1.0
OD1 B:ASP44 4.0 42.5 1.0
ND1 B:HIS98 4.0 52.4 1.0
CG B:HIS98 4.1 51.0 1.0
N B:GLY102 4.1 42.0 1.0
C B:CYS101 4.2 43.0 1.0
O B:HOH2244 4.2 41.1 1.0
CA B:ASP44 4.4 49.1 1.0
N B:ASP44 4.4 46.7 1.0
N B:GLY103 4.4 44.9 1.0
CA B:CYS42 4.7 40.7 1.0
OD1 B:ASN68 4.9 35.0 1.0
CA B:ALA67 4.9 37.3 1.0
N B:CYS101 4.9 46.9 1.0
N B:ALA67 4.9 38.4 1.0

Zinc binding site 3 out of 6 in 2a8c

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Zinc binding site 3 out of 6 in the Haemophilus Influenzae Beta-Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Haemophilus Influenzae Beta-Carbonic Anhydrase within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn3230

b:53.6
occ:1.00
SG C:CYS101 2.1 49.4 1.0
SG C:CYS42 2.2 58.0 1.0
OD2 C:ASP44 2.2 59.4 1.0
NE2 C:HIS98 2.2 59.1 1.0
CE1 C:HIS98 2.6 57.4 1.0
CB C:CYS42 3.1 52.8 1.0
CG C:ASP44 3.1 57.3 1.0
CB C:CYS101 3.3 56.4 1.0
CD2 C:HIS98 3.4 57.7 1.0
CB C:ASP44 3.5 56.1 1.0
CA C:CYS101 3.8 56.8 1.0
ND1 C:HIS98 3.8 57.0 1.0
N C:GLY102 4.0 55.7 1.0
CG C:HIS98 4.2 56.9 1.0
OD1 C:ASP44 4.2 60.1 1.0
C C:CYS101 4.2 56.3 1.0
N C:GLY103 4.4 52.0 1.0
N C:ASP44 4.5 53.0 1.0
CA C:CYS42 4.5 51.9 1.0
CA C:ASP44 4.6 55.8 1.0
CA C:ALA67 4.7 39.0 1.0
N C:ALA67 4.7 40.7 1.0
C C:CYS42 4.9 52.0 1.0

Zinc binding site 4 out of 6 in 2a8c

Go back to Zinc Binding Sites List in 2a8c
Zinc binding site 4 out of 6 in the Haemophilus Influenzae Beta-Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Haemophilus Influenzae Beta-Carbonic Anhydrase within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn4230

b:43.0
occ:1.00
OD2 D:ASP44 1.9 42.3 1.0
NE2 D:HIS98 2.0 36.8 1.0
SG D:CYS101 2.3 41.0 1.0
SG D:CYS42 2.3 40.0 1.0
CE1 D:HIS98 2.8 36.2 1.0
CG D:ASP44 2.9 44.0 1.0
CD2 D:HIS98 3.1 34.3 1.0
CB D:CYS42 3.2 28.6 1.0
CB D:ASP44 3.3 41.2 1.0
CB D:CYS101 3.3 44.4 1.0
CA D:CYS101 3.6 42.9 1.0
ND1 D:HIS98 4.0 38.0 1.0
OD1 D:ASP44 4.0 41.1 1.0
N D:GLY102 4.1 42.6 1.0
CG D:HIS98 4.1 37.0 1.0
O D:HOH4249 4.1 35.1 1.0
C D:CYS101 4.2 44.0 1.0
N D:ASP44 4.3 40.3 1.0
N D:GLY103 4.3 41.2 1.0
CA D:ASP44 4.4 43.6 1.0
CA D:CYS42 4.7 34.6 1.0
CA D:ALA67 4.9 33.3 1.0
N D:ALA67 4.9 33.4 1.0
N D:CYS101 4.9 48.5 1.0
C D:CYS42 5.0 36.0 1.0

Zinc binding site 5 out of 6 in 2a8c

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Zinc binding site 5 out of 6 in the Haemophilus Influenzae Beta-Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Haemophilus Influenzae Beta-Carbonic Anhydrase within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn5230

b:57.4
occ:1.00
SG E:CYS101 2.0 49.5 1.0
NE2 E:HIS98 2.1 76.7 1.0
OD2 E:ASP44 2.1 63.3 1.0
SG E:CYS42 2.2 59.4 1.0
CE1 E:HIS98 2.6 75.3 1.0
CG E:ASP44 3.0 62.6 1.0
CD2 E:HIS98 3.2 75.0 1.0
CB E:CYS42 3.2 56.1 1.0
CB E:CYS101 3.3 56.0 1.0
CB E:ASP44 3.4 61.2 1.0
ND1 E:HIS98 3.7 74.5 1.0
CA E:CYS101 3.8 55.9 1.0
CG E:HIS98 4.0 74.3 1.0
OD1 E:ASP44 4.1 66.0 1.0
N E:GLY102 4.3 53.2 1.0
C E:CYS101 4.3 54.2 1.0
N E:ASP44 4.5 60.0 1.0
N E:GLY103 4.5 49.1 1.0
CA E:ASP44 4.6 62.6 1.0
CA E:CYS42 4.6 57.3 1.0
N E:ALA67 4.7 46.1 1.0
CA E:ALA67 4.7 42.9 1.0

Zinc binding site 6 out of 6 in 2a8c

Go back to Zinc Binding Sites List in 2a8c
Zinc binding site 6 out of 6 in the Haemophilus Influenzae Beta-Carbonic Anhydrase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 6 of Haemophilus Influenzae Beta-Carbonic Anhydrase within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Zn6230

b:50.1
occ:1.00
OD2 F:ASP44 1.9 44.8 1.0
NE2 F:HIS98 1.9 48.1 1.0
SG F:CYS101 2.3 45.4 1.0
SG F:CYS42 2.3 39.8 1.0
CE1 F:HIS98 2.7 50.9 1.0
CG F:ASP44 2.8 45.4 1.0
CD2 F:HIS98 3.0 48.8 1.0
CB F:CYS101 3.1 47.4 1.0
CB F:CYS42 3.2 39.1 1.0
CB F:ASP44 3.2 44.0 1.0
CA F:CYS101 3.6 47.5 1.0
ND1 F:HIS98 3.9 49.3 1.0
OD1 F:ASP44 4.0 46.0 1.0
CG F:HIS98 4.0 48.8 1.0
N F:GLY102 4.1 45.5 1.0
O F:HOH6248 4.1 41.3 1.0
C F:CYS101 4.2 46.9 1.0
N F:ASP44 4.4 45.8 1.0
CA F:ASP44 4.4 45.7 1.0
N F:GLY103 4.4 45.1 1.0
CA F:CYS42 4.6 40.7 1.0
N F:ALA67 4.8 38.8 1.0
CA F:ALA67 4.9 38.9 1.0
N F:CYS101 4.9 51.0 1.0
OD1 F:ASN68 5.0 40.5 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 03:17:00 2020

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