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Zinc in PDB 5ca2: Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II

Enzymatic activity of Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II

All present enzymatic activity of Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II, PDB code: 5ca2 was solved by R.S.Alexander, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.700, 41.700, 73.000, 90.00, 104.60, 90.00
R / Rfree (%) n/a / n/a

Other elements in 5ca2:

The structure of Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II also contains other interesting chemical elements:

Mercury (Hg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II (pdb code 5ca2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II, PDB code: 5ca2:

Zinc binding site 1 out of 1 in 5ca2

Go back to Zinc Binding Sites List in 5ca2
Zinc binding site 1 out of 1 in the Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Conformational Mobility of His-64 in the Thr-200 (Right Arrow) Ser Mutant of Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:7.9
occ:1.00
 ND1 A:HIS119 2.1 5.5 1.0
NE2 A:HIS94 2.2 3.6 1.0
NE2 A:HIS96 2.2 3.9 1.0
O A:HOH379 2.8 2.2 1.0
CE1 A:HIS119 2.9 5.4 1.0
CD2 A:HIS94 3.0 4.1 1.0
CD2 A:HIS96 3.1 4.1 1.0
CE1 A:HIS96 3.2 4.2 1.0
CG A:HIS119 3.2 5.2 1.0
CE1 A:HIS94 3.3 3.9 1.0
CB A:HIS119 3.7 5.2 1.0
OG1 A:THR199 3.9 4.6 1.0
OE1 A:GLU106 4.0 5.7 1.0
NE2 A:HIS119 4.2 5.3 1.0
CG A:HIS96 4.3 4.5 1.0
CG A:HIS94 4.3 4.3 1.0
CD2 A:HIS119 4.3 5.1 1.0
ND1 A:HIS96 4.3 4.2 1.0
ND1 A:HIS94 4.4 4.1 1.0
O A:HOH335 4.8 24.9 1.0
CD A:GLU106 4.9 5.6 1.0

Reference:

J.F.Krebs, C.A.Fierke, R.S.Alexander, D.W.Christianson. Conformational Mobility of His-64 in the Thr-200----Ser Mutant of Human Carbonic Anhydrase II. Biochemistry V. 30 9153 1991.
ISSN: ISSN 0006-2960
PubMed: 1909891
DOI: 10.1021/BI00102A005
Page generated: Sun Oct 27 14:00:40 2024

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