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

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

All present enzymatic activity of Human Carbonic Anhydrase II[Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Ser (A65S)-Orthorhombic Form:
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)-Orthorhombic Form, PDB code: 1ugg 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 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 42.500, 72.700, 75.100, 90.00, 90.00, 90.00
R / Rfree (%) 17.9 / 28.2

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)-Orthorhombic Form (pdb code 1ugg). 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)-Orthorhombic Form, PDB code: 1ugg:

Zinc binding site 1 out of 1 in 1ugg

Go back to Zinc Binding Sites List in 1ugg
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)-Orthorhombic Form


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)-Orthorhombic Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:15.2
occ:1.00
 ND1 A:HIS119 2.0 6.5 1.0
NE2 A:HIS94 2.0 4.1 1.0
NE2 A:HIS96 2.1 7.1 1.0
CE1 A:HIS119 2.6 6.1 1.0
CD2 A:HIS94 2.8 6.8 1.0
CD2 A:HIS96 3.0 5.7 1.0
CE1 A:HIS94 3.1 4.6 1.0
CE1 A:HIS96 3.1 6.8 1.0
CG A:HIS119 3.2 5.2 1.0
OG1 A:THR199 3.6 7.2 1.0
CB A:HIS119 3.8 4.0 1.0
NE2 A:HIS119 3.8 5.3 1.0
OE1 A:GLU106 4.0 10.8 1.0
CG A:HIS94 4.1 9.9 1.0
ND1 A:HIS94 4.1 10.2 1.0
CD2 A:HIS119 4.2 2.9 1.0
CG A:HIS96 4.2 9.5 1.0
ND1 A:HIS96 4.2 9.0 1.0
O A:HOH408 4.3 36.5 1.0
O A:HOH402 4.4 38.5 1.0
CD A:GLU106 4.9 7.3 1.0
CB A:THR199 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 19:31:43 2024

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