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Zinc in PDB 1g0e: Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole

Enzymatic activity of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole

All present enzymatic activity of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole:
4.2.1.1;

Protein crystallography data

The structure of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole, PDB code: 1g0e was solved by D.Duda, R.Mckenna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.00 / 1.60
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.142, 41.490, 72.063, 90.00, 104.28, 90.00
R / Rfree (%) 17.9 / 20

Other elements in 1g0e:

The structure of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole also contains other interesting chemical elements:

Mercury (Hg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole (pdb code 1g0e). 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 Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole, PDB code: 1g0e:

Zinc binding site 1 out of 1 in 1g0e

Go back to Zinc Binding Sites List in 1g0e
Zinc binding site 1 out of 1 in the Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Site-Specific Mutant (HIS64 Replaced with Ala) of Human Carbonic Anhydrase II Complexed with 4-Methylimidazole within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:4.3
occ:1.00
O A:HOH574 1.8 13.1 1.0
NE2 A:HIS96 2.0 3.2 1.0
ND1 A:HIS119 2.1 2.5 1.0
NE2 A:HIS94 2.1 3.2 1.0
CE1 A:HIS119 2.9 2.6 1.0
CD2 A:HIS96 3.0 3.8 1.0
CD2 A:HIS94 3.0 3.2 1.0
CE1 A:HIS96 3.1 3.9 1.0
CE1 A:HIS94 3.2 4.0 1.0
CG A:HIS119 3.2 2.1 1.0
OG1 A:THR199 3.6 4.5 1.0
CB A:HIS119 3.6 2.1 1.0
O A:HOH394 3.8 15.6 1.0
OE2 A:GLU106 3.9 3.0 1.0
O A:HOH399 4.0 28.1 1.0
NE2 A:HIS119 4.1 1.5 1.0
CG A:HIS96 4.1 3.2 1.0
ND1 A:HIS96 4.2 3.9 1.0
CG A:HIS94 4.2 3.0 1.0
ND1 A:HIS94 4.2 2.5 1.0
CD2 A:HIS119 4.2 2.6 1.0
O A:HOH395 4.5 13.1 1.0
CD A:GLU106 4.8 3.8 1.0
O A:HOH398 4.8 23.6 1.0
CB A:THR199 5.0 4.2 1.0

Reference:

D.Duda, C.Tu, M.Qian, P.Laipis, M.Agbandje-Mckenna, D.N.Silverman, R.Mckenna. Structural and Kinetic Analysis of the Chemical Rescue of the Proton Transfer Function of Carbonic Anhydrase II. Biochemistry V. 40 1741 2001.
ISSN: ISSN 0006-2960
PubMed: 11327835
DOI: 10.1021/BI002295Z
Page generated: Wed Dec 16 02:49:44 2020

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