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Zinc in PDB 1ugd: Human Carbonic Anhydrase II[Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Ser (A65S)

Enzymatic activity of Human Carbonic Anhydrase II[Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Ser (A65S)

All present enzymatic activity of Human Carbonic Anhydrase II[Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Ser (A65S):
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 Ser (A65S), PDB code: 1ugd 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 (%) 17.6 / 25.5

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 Ser (A65S) (pdb code 1ugd). 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 Ser (A65S), PDB code: 1ugd:

Zinc binding site 1 out of 1 in 1ugd

Go back to Zinc Binding Sites List in 1ugd
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 Ser (A65S)


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 Ser (A65S) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:12.1
occ:1.00
 NE2 A:HIS94 1.9 6.4 1.0
O A:HOH263 2.0 15.0 1.0
ND1 A:HIS119 2.0 8.9 1.0
NE2 A:HIS96 2.1 11.0 1.0
CE1 A:HIS119 2.8 6.5 1.0
CD2 A:HIS94 2.9 10.1 1.0
CD2 A:HIS96 2.9 6.6 1.0
CE1 A:HIS94 3.0 5.9 1.0
CG A:HIS119 3.1 9.3 1.0
CE1 A:HIS96 3.2 4.7 1.0
CB A:HIS119 3.6 7.3 1.0
O A:HOH338 3.7 26.9 1.0
OG1 A:THR199 3.8 7.5 1.0
NE2 A:HIS119 4.0 10.2 1.0
CG A:HIS94 4.1 5.7 1.0
ND1 A:HIS94 4.1 5.3 1.0
O A:HOH292 4.1 29.8 1.0
CG A:HIS96 4.2 9.3 1.0
OE1 A:GLU106 4.2 8.6 1.0
CD2 A:HIS119 4.2 8.4 1.0
ND1 A:HIS96 4.3 7.5 1.0
CD A:GLU106 5.0 11.4 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 Oct 16 19:31:05 2024

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