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Mercury in PDB 1uge: Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Leu (A65L)

Enzymatic activity of Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Leu (A65L)

All present enzymatic activity of Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Leu (A65L):
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 Leu (A65L), PDB code: 1uge 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 / 1.90
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 (%) 17.4 / 22.9

Other elements in 1uge:

The structure of Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Leu (A65L) also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Leu (A65L) (pdb code 1uge). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total only one binding site of Mercury was determined in the Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Leu (A65L), PDB code: 1uge:

Mercury binding site 1 out of 1 in 1uge

Go back to Mercury Binding Sites List in 1uge
Mercury 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 Leu (A65L)


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By Leu (A65L) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg483

b:22.4
occ:1.00
CB A:CYS206 2.9 20.9 1.0
O A:GLN137 3.2 15.3 1.0
O A:GLU205 3.2 15.8 1.0
O A:HOH362 3.4 27.3 1.0
CA A:CYS206 3.5 16.1 1.0
C A:GLN137 3.5 16.6 1.0
O A:VAL135 3.6 16.5 1.0
C A:GLU205 3.6 14.8 1.0
N A:GLN137 3.8 17.5 1.0
N A:CYS206 3.8 14.9 1.0
SG A:CYS206 3.8 40.9 1.0
O A:HOH331 3.9 20.9 1.0
C A:VAL135 4.0 17.1 1.0
C A:GLN136 4.1 18.2 1.0
N A:PRO138 4.1 15.7 1.0
CA A:GLN137 4.2 16.3 1.0
CA A:PRO138 4.4 15.0 1.0
N A:GLN136 4.4 16.5 1.0
CA A:GLN136 4.4 17.3 1.0
O A:HOH365 4.4 24.2 1.0
N A:GLU205 4.5 15.7 1.0
O A:GLN136 4.6 17.9 1.0
CA A:GLU205 4.6 14.6 1.0
CA A:VAL135 4.8 16.8 1.0
CB A:LEU204 4.9 19.4 1.0
C A:CYS206 5.0 13.1 1.0
O A:ALA134 5.0 17.8 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: Sun Dec 13 19:05:23 2020

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