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Zinc in PDB 4c3t: The Carbonic Anhydrase From Thermovibrio Ammonificans Reveals An Interesting Intermolecular Disulfide Contributing to Increasing Thermal Stability of This Enzyme

Enzymatic activity of The Carbonic Anhydrase From Thermovibrio Ammonificans Reveals An Interesting Intermolecular Disulfide Contributing to Increasing Thermal Stability of This Enzyme

All present enzymatic activity of The Carbonic Anhydrase From Thermovibrio Ammonificans Reveals An Interesting Intermolecular Disulfide Contributing to Increasing Thermal Stability of This Enzyme:
4.2.1.1;

Protein crystallography data

The structure of The Carbonic Anhydrase From Thermovibrio Ammonificans Reveals An Interesting Intermolecular Disulfide Contributing to Increasing Thermal Stability of This Enzyme, PDB code: 4c3t was solved by P.James, M.Isupov, C.Sayer, S.Berg, M.Lioliou, H.Kotlar, J.Littlechild, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 57.23 / 1.69
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 80.930, 80.930, 154.620, 90.00, 90.00, 90.00
R / Rfree (%) 22.13 / 25.175

Other elements in 4c3t:

The structure of The Carbonic Anhydrase From Thermovibrio Ammonificans Reveals An Interesting Intermolecular Disulfide Contributing to Increasing Thermal Stability of This Enzyme also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the The Carbonic Anhydrase From Thermovibrio Ammonificans Reveals An Interesting Intermolecular Disulfide Contributing to Increasing Thermal Stability of This Enzyme (pdb code 4c3t). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the The Carbonic Anhydrase From Thermovibrio Ammonificans Reveals An Interesting Intermolecular Disulfide Contributing to Increasing Thermal Stability of This Enzyme, PDB code: 4c3t:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4c3t

Go back to Zinc Binding Sites List in 4c3t
Zinc binding site 1 out of 2 in the The Carbonic Anhydrase From Thermovibrio Ammonificans Reveals An Interesting Intermolecular Disulfide Contributing to Increasing Thermal Stability of This Enzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of The Carbonic Anhydrase From Thermovibrio Ammonificans Reveals An Interesting Intermolecular Disulfide Contributing to Increasing Thermal Stability of This Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn300

b:20.2
occ:1.00
 O A:HOH2115 2.0 27.7 1.0
NE2 A:HIS112 2.0 18.3 1.0
ND1 A:HIS131 2.1 19.1 1.0
NE2 A:HIS114 2.1 13.2 1.0
CD2 A:HIS114 2.9 20.5 1.0
CD2 A:HIS112 2.9 14.3 1.0
CE1 A:HIS131 3.0 14.3 1.0
CE1 A:HIS112 3.1 22.3 1.0
CG A:HIS131 3.1 15.0 1.0
CE1 A:HIS114 3.1 24.0 1.0
CB A:HIS131 3.5 16.1 1.0
O A:HOH2114 3.6 24.3 1.0
OE1 A:GLU118 3.8 19.6 1.0
OG1 A:THR198 3.8 18.8 1.0
CG A:HIS112 4.1 19.1 1.0
NE2 A:HIS131 4.1 15.7 1.0
ND1 A:HIS112 4.1 19.5 1.0
CG A:HIS114 4.1 16.6 1.0
ND1 A:HIS114 4.2 16.9 1.0
CD2 A:HIS131 4.2 18.6 1.0
O A:HOH2179 4.2 29.6 1.0
O A:HOH2013 4.6 26.1 1.0
CD A:GLU118 4.7 25.4 1.0
CA A:HIS131 5.0 14.3 1.0

Zinc binding site 2 out of 2 in 4c3t

Go back to Zinc Binding Sites List in 4c3t
Zinc binding site 2 out of 2 in the The Carbonic Anhydrase From Thermovibrio Ammonificans Reveals An Interesting Intermolecular Disulfide Contributing to Increasing Thermal Stability of This Enzyme


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of The Carbonic Anhydrase From Thermovibrio Ammonificans Reveals An Interesting Intermolecular Disulfide Contributing to Increasing Thermal Stability of This Enzyme within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn300

b:32.6
occ:0.70
 O B:HOH2040 1.9 20.6 1.0
NE2 B:HIS114 2.1 35.0 1.0
ND1 B:HIS131 2.1 42.2 1.0
NE2 B:HIS112 2.1 33.2 1.0
CD2 B:HIS112 2.8 41.1 1.0
CD2 B:HIS114 2.9 40.9 1.0
CE1 B:HIS131 3.0 43.5 1.0
CG B:HIS131 3.1 38.2 1.0
CE1 B:HIS114 3.2 38.4 1.0
CE1 B:HIS112 3.2 39.6 1.0
CB B:HIS131 3.5 32.5 1.0
OE1 B:GLU118 3.7 49.5 1.0
OG1 B:THR198 3.8 41.8 1.0
CG B:HIS112 4.0 39.4 1.0
CG B:HIS114 4.1 41.7 1.0
NE2 B:HIS131 4.1 37.8 1.0
ND1 B:HIS112 4.2 39.1 1.0
ND1 B:HIS114 4.2 38.3 1.0
CD2 B:HIS131 4.2 41.8 1.0
O B:HOH2064 4.6 50.2 1.0
CD B:GLU118 4.7 47.2 1.0
CA B:HIS131 4.9 29.9 1.0

Reference:

P.James, M.N.Isupov, C.Sayer, V.Saneei, S.Berg, M.Lioliou, H.Kotlar, J.Littlechild. The Structure of A Tetrameric [Alpha]-Carbonic Anhydrase From Thermovibrio Ammonificans Reveals A Core Formed Around Intermolecular Disulfides That Contribute to Its Thermostability Acta Crystallogr.,Sect.D V. 70 2607 2014.
ISSN: ISSN 0907-4449
PubMed: 25286845
DOI: 10.1107/S1399004714016526
Page generated: Wed Dec 16 05:07:40 2020

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