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Zinc in PDB 6sc4: Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp.

Protein crystallography data

The structure of Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp., PDB code: 6sc4 was solved by M.Vogler, R.Karan, D.Renn, A.Vancea, V.-T.Vielberg, S.W.Groetzinger, P.Dassarma, S.Das Sarma, J.Eppinger, M.Groll, M.Rueping, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 2.60
Space group F 4 3 2 4
Cell size a, b, c (Å), α, β, γ (°) 362.640, 362.640, 362.640, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.4

Other elements in 6sc4:

The structure of Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp. also contains other interesting chemical elements:

Cadmium (Cd) 13 atoms
Sodium (Na) 7 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp. (pdb code 6sc4). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 5 binding sites of Zinc where determined in the Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp., PDB code: 6sc4:
Jump to Zinc binding site number: 1; 2; 3; 4; 5;

Zinc binding site 1 out of 5 in 6sc4

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Zinc binding site 1 out of 5 in the Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn901

b:30.6
occ:1.00
O A:HOH1024 2.0 37.1 1.0
NE2 A:HIS94 2.0 41.2 1.0
ND1 A:HIS64 2.1 38.3 1.0
NE2 B:HIS89 2.2 32.6 1.0
NZ B:LYS58 2.9 44.9 1.0
CE1 A:HIS64 3.0 38.4 1.0
CD2 A:HIS94 3.0 40.9 1.0
CE1 A:HIS94 3.0 41.7 1.0
CE1 B:HIS89 3.1 32.9 1.0
CD2 B:HIS89 3.2 33.0 1.0
CG A:HIS64 3.2 38.1 1.0
CE B:LYS58 3.6 45.4 1.0
CB A:HIS64 3.7 38.4 1.0
O A:PRO65 3.9 44.5 1.0
ND1 A:HIS94 4.1 41.6 1.0
NE2 A:HIS64 4.1 37.7 1.0
CG A:HIS94 4.2 40.8 1.0
ND1 B:HIS89 4.2 32.5 1.0
CD2 A:HIS64 4.3 38.2 1.0
CD B:LYS58 4.3 44.4 1.0
CG B:HIS89 4.3 34.0 1.0
O B:HOH1069 4.6 25.9 1.0
OD1 A:ASP67 4.6 45.5 1.0
CE1 B:HIS166 4.9 52.0 1.0
C A:PRO65 5.0 43.9 1.0
CA A:HIS64 5.0 38.5 1.0
C A:HIS64 5.0 39.7 1.0

Zinc binding site 2 out of 5 in 6sc4

Go back to Zinc Binding Sites List in 6sc4
Zinc binding site 2 out of 5 in the Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn907

b:34.7
occ:1.00
NE2 C:HIS94 2.0 43.1 1.0
ND1 C:HIS64 2.2 41.2 1.0
NE2 A:HIS89 2.2 41.5 1.0
O C:HOH1019 2.2 49.7 1.0
CE1 C:HIS64 2.9 41.4 1.0
NZ A:LYS58 3.0 47.3 1.0
CE1 C:HIS94 3.0 43.7 1.0
CD2 C:HIS94 3.0 43.4 1.0
CE1 A:HIS89 3.2 41.5 1.0
CD2 A:HIS89 3.2 41.9 1.0
CG C:HIS64 3.3 41.3 1.0
CB C:HIS64 3.8 41.5 1.0
O C:PRO65 3.9 39.8 1.0
CD A:LYS58 4.0 45.7 1.0
CE A:LYS58 4.0 47.4 1.0
ND1 C:HIS94 4.1 43.7 1.0
NE2 C:HIS64 4.1 41.3 1.0
CG C:HIS94 4.1 43.6 1.0
ND1 A:HIS89 4.3 40.9 1.0
CD2 C:HIS64 4.3 41.1 1.0
CG A:HIS89 4.4 41.2 1.0
OD2 C:ASP67 4.6 46.8 1.0
O A:HOH1059 4.8 29.0 1.0
CE1 A:HIS166 5.0 53.4 1.0
C C:PRO65 5.0 40.9 1.0

Zinc binding site 3 out of 5 in 6sc4

Go back to Zinc Binding Sites List in 6sc4
Zinc binding site 3 out of 5 in the Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn901

b:29.0
occ:1.00
O B:HOH1030 2.0 42.1 1.0
NE2 B:HIS94 2.1 38.0 1.0
ND1 B:HIS64 2.2 35.4 1.0
NE2 C:HIS89 2.2 39.2 1.0
CE1 B:HIS64 2.9 35.8 1.0
NZ C:LYS58 3.0 48.8 1.0
CD2 B:HIS94 3.1 38.1 1.0
CE1 C:HIS89 3.2 39.2 1.0
CE1 B:HIS94 3.2 38.2 1.0
CD2 C:HIS89 3.2 39.5 1.0
CG B:HIS64 3.3 35.5 1.0
CB B:HIS64 3.8 36.3 1.0
O B:PRO65 3.9 41.0 1.0
CE C:LYS58 3.9 48.4 1.0
NE2 B:HIS64 4.1 34.9 1.0
CD C:LYS58 4.2 46.2 1.0
CG B:HIS94 4.2 37.3 1.0
ND1 B:HIS94 4.3 37.6 1.0
ND1 C:HIS89 4.3 38.8 1.0
CG C:HIS89 4.3 39.3 1.0
CD2 B:HIS64 4.3 35.0 1.0
OD1 B:ASP67 4.6 41.0 1.0
O C:HOH1064 4.7 25.1 1.0
CE1 C:HIS166 4.9 43.4 1.0
C B:PRO65 5.0 40.1 1.0

Zinc binding site 4 out of 5 in 6sc4

Go back to Zinc Binding Sites List in 6sc4
Zinc binding site 4 out of 5 in the Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp. within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Zn202

b:26.0
occ:1.00
NE2 D:HIS94 2.1 31.0 1.0
ND1 D:HIS64 2.1 33.8 1.0
CE1 D:HIS64 2.9 33.7 1.0
CE1 D:HIS94 3.0 31.2 1.0
CD2 D:HIS94 3.1 31.4 1.0
CG D:HIS64 3.3 32.8 1.0
CB D:HIS64 3.8 32.8 1.0
O D:PRO65 3.8 33.7 1.0
NE2 D:HIS64 4.1 33.3 1.0
ND1 D:HIS94 4.1 30.6 1.0
OD1 D:ASP67 4.2 38.1 1.0
CG D:HIS94 4.2 30.9 1.0
CD2 D:HIS64 4.3 32.6 1.0
C D:PRO65 4.9 32.6 1.0
O D:HIS64 5.0 32.8 1.0
C D:HIS64 5.0 32.4 1.0

Zinc binding site 5 out of 5 in 6sc4

Go back to Zinc Binding Sites List in 6sc4
Zinc binding site 5 out of 5 in the Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 5 of Gamma-Carbonic Anhydrase From the Haloarchaeon Halobacterium Sp. within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Zn901

b:24.4
occ:1.00
NE2 E:HIS94 2.1 29.0 1.0
ND1 E:HIS64 2.1 33.2 1.0
O E:HOH1024 2.2 32.1 1.0
CE1 E:HIS64 2.9 33.5 1.0
CE1 E:HIS94 3.1 29.4 1.0
CD2 E:HIS94 3.1 29.5 1.0
CG E:HIS64 3.3 32.6 1.0
CB E:HIS64 3.8 31.8 1.0
O E:PRO65 3.8 30.4 1.0
NE2 E:HIS64 4.1 33.0 1.0
ND1 E:HIS94 4.2 29.2 1.0
CG E:HIS94 4.2 29.4 1.0
CD2 E:HIS64 4.3 32.8 1.0
OD2 E:ASP67 4.6 37.3 1.0
C E:PRO65 4.9 30.9 1.0

Reference:

M.Vogler, R.Karan, D.Renn, A.Vancea, V.-T.Vielberg, S.W.Groetzinger, P.Dassarma, S.Das Sarma, J.Eppinger, M.Groll, M.Rueping. Crystal Structure and Active Site Engineering of A Halophilic Gamma-Carbonic Anhydrase Front Microbiol 2020.
ISSN: ESSN 1664-302X
DOI: 10.3389/FMICB.2020.00742
Page generated: Tue Oct 29 07:08:19 2024

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