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Zinc in PDB 1rj5: Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase Xiv

Enzymatic activity of Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase Xiv

All present enzymatic activity of Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase Xiv:
4.2.1.1;

Protein crystallography data

The structure of Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase Xiv, PDB code: 1rj5 was solved by D.A.Whittington, J.H.Grubb, A.Waheed, G.N.Shah, W.S.Sly, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.81
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.000, 75.600, 73.200, 90.00, 98.90, 90.00
R / Rfree (%) 23.4 / 27.4

Other elements in 1rj5:

The structure of Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase Xiv also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase Xiv (pdb code 1rj5). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase Xiv, PDB code: 1rj5:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 1rj5

Go back to Zinc Binding Sites List in 1rj5
Zinc binding site 1 out of 2 in the Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase Xiv


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase Xiv within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn601

b:31.6
occ:1.00
O A:HOH824 2.0 36.0 1.0
NE2 A:HIS96 2.1 22.5 1.0
ND1 A:HIS119 2.1 27.8 1.0
O A:ACY701 2.1 40.9 1.0
NE2 A:HIS94 2.3 38.8 1.0
CE1 A:HIS96 3.0 24.3 1.0
CE1 A:HIS119 3.0 26.1 1.0
CD2 A:HIS94 3.1 37.6 1.0
CG A:HIS119 3.1 27.9 1.0
CD2 A:HIS96 3.1 23.7 1.0
CE1 A:HIS94 3.3 38.8 1.0
C A:ACY701 3.4 41.7 1.0
CB A:HIS119 3.4 27.4 1.0
OG1 A:THR199 3.8 29.5 1.0
CH3 A:ACY701 4.0 41.0 1.0
ND1 A:HIS96 4.1 26.5 1.0
NE2 A:HIS119 4.1 26.2 1.0
CD2 A:HIS119 4.2 27.2 1.0
CG A:HIS96 4.2 27.2 1.0
CG A:HIS94 4.2 38.7 1.0
ND1 A:HIS94 4.3 39.5 1.0
OXT A:ACY701 4.3 43.3 1.0
OE2 A:GLU106 4.4 38.8 1.0
CA A:HIS119 4.9 28.4 1.0
CD A:GLU106 4.9 39.9 1.0
OE1 A:GLU106 5.0 40.9 1.0

Zinc binding site 2 out of 2 in 1rj5

Go back to Zinc Binding Sites List in 1rj5
Zinc binding site 2 out of 2 in the Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase Xiv


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Extracellular Domain of Murine Carbonic Anhydrase Xiv within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn601

b:33.3
occ:1.00
NE2 B:HIS96 2.0 18.9 1.0
O B:ACY702 2.0 17.8 1.0
ND1 B:HIS119 2.1 29.7 1.0
O B:HOH910 2.3 6.2 1.0
NE2 B:HIS94 2.3 38.3 1.0
CE1 B:HIS96 2.9 21.5 1.0
CE1 B:HIS119 3.0 26.8 1.0
CD2 B:HIS96 3.0 21.5 1.0
CD2 B:HIS94 3.1 37.1 1.0
CG B:HIS119 3.1 29.2 1.0
C B:ACY702 3.3 19.6 1.0
CE1 B:HIS94 3.4 37.0 1.0
CB B:HIS119 3.4 29.4 1.0
OG1 B:THR199 3.8 32.2 1.0
ND1 B:HIS96 4.0 24.3 1.0
OXT B:ACY702 4.1 21.5 1.0
CG B:HIS96 4.1 24.8 1.0
NE2 B:HIS119 4.1 27.1 1.0
CD2 B:HIS119 4.2 28.9 1.0
CG B:HIS94 4.2 37.1 1.0
CH3 B:ACY702 4.3 18.2 1.0
OE2 B:GLU106 4.3 38.3 1.0
ND1 B:HIS94 4.4 37.2 1.0
O B:HOH909 4.8 12.8 1.0
CD B:GLU106 4.9 39.2 1.0
CA B:HIS119 4.9 29.3 1.0
OE1 B:GLU106 5.0 40.0 1.0

Reference:

D.A.Whittington, J.H.Grubb, A.Waheed, G.N.Shah, W.S.Sly, D.W.Christianson. Expression, Assay, and Structure of the Extracellular Domain of Murine Carbonic Anhydrase Xiv: Implications For Selective Inhibition of Membrane-Associated Isozymes. J.Biol.Chem. V. 279 7223 2004.
ISSN: ISSN 0021-9258
PubMed: 14660577
DOI: 10.1074/JBC.M310809200
Page generated: Wed Dec 16 03:02:57 2020

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