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Zinc in PDB 1uga: Human Carbonic Anhydrase II[Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Phe (A65F)

Enzymatic activity of Human Carbonic Anhydrase II[Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Phe (A65F)

All present enzymatic activity of Human Carbonic Anhydrase II[Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Phe (A65F):
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II[Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Phe (A65F), PDB code: 1uga was solved by L.R.Scolnick, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.50 / 2.00
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 (%) 15.4 / 24.6

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Carbonic Anhydrase II[Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Phe (A65F) (pdb code 1uga). 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 Human Carbonic Anhydrase II[Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Phe (A65F), PDB code: 1uga:

Zinc binding site 1 out of 1 in 1uga

Go back to Zinc Binding Sites List in 1uga
Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II[Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Phe (A65F)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Carbonic Anhydrase II[Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Phe (A65F) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:17.2
occ:1.00
 NE2 A:HIS96 2.0 8.7 1.0
ND1 A:HIS119 2.0 3.5 1.0
NE2 A:HIS94 2.1 20.4 1.0
O A:HOH263 2.5 42.4 1.0
CE1 A:HIS119 2.6 2.0 1.0
CD2 A:HIS94 2.8 15.9 1.0
CD2 A:HIS96 2.9 5.8 1.0
CE1 A:HIS96 3.1 8.1 1.0
O A:HOH319 3.2 48.2 1.0
CE1 A:HIS94 3.2 15.2 1.0
CG A:HIS119 3.3 9.2 1.0
OG1 A:THR199 3.6 17.9 1.0
CB A:HIS119 3.8 7.9 1.0
NE2 A:HIS119 3.9 5.3 1.0
OE1 A:GLU106 4.0 13.0 1.0
CG A:HIS94 4.1 14.6 1.0
CG A:HIS96 4.2 12.2 1.0
ND1 A:HIS96 4.2 8.9 1.0
CD2 A:HIS119 4.2 3.1 1.0
ND1 A:HIS94 4.2 11.8 1.0
CE2 A:PHE65 4.9 24.9 1.0
CD A:GLU106 4.9 12.8 1.0
CB A:THR199 5.0 10.0 1.0

Reference:

L.R.Scolnick, D.W.Christianson. X-Ray Crystallographic Studies of Alanine-65 Variants of Carbonic Anhydrase II Reveal the Structural Basis of Compromised Proton Transfer in Catalysis. Biochemistry V. 35 16429 1996.
ISSN: ISSN 0006-2960
PubMed: 8987974
DOI: 10.1021/BI9617872
Page generated: Wed Dec 16 03:06:36 2020

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