Atomistry » Mercury » PDB 1rsv-1yp2 » 1ugc
Atomistry »
  Mercury »
    PDB 1rsv-1yp2 »
      1ugc »

Mercury in PDB 1ugc: Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By His (A65H)

Enzymatic activity of Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By His (A65H)

All present enzymatic activity of Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By His (A65H):
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 His (A65H), PDB code: 1ugc 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 (%) 16.2 / 22.5

Other elements in 1ugc:

The structure of Human Carbonic Anhydrase II [Hcaii] (E.C.4.2.1.1) Mutant with Ala 65 Replaced By His (A65H) 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 His (A65H) (pdb code 1ugc). 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 His (A65H), PDB code: 1ugc:

Mercury binding site 1 out of 1 in 1ugc

Go back to Mercury Binding Sites List in 1ugc
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 His (A65H)


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 His (A65H) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg483

b:20.9
occ:1.00
CB A:CYS206 2.9 19.5 1.0
O A:GLN137 3.1 8.9 1.0
O A:GLU205 3.3 11.2 1.0
C A:GLN137 3.4 11.8 1.0
CA A:CYS206 3.5 13.9 1.0
C A:GLU205 3.6 12.0 1.0
O A:VAL135 3.6 12.7 1.0
N A:GLN137 3.7 16.2 1.0
N A:CYS206 3.7 10.0 1.0
O A:HOH361 3.8 36.3 1.0
SG A:CYS206 3.9 39.7 1.0
C A:GLN136 3.9 15.1 1.0
O A:HOH330 4.0 15.6 1.0
C A:VAL135 4.0 13.5 1.0
N A:PRO138 4.1 10.2 1.0
CA A:GLN137 4.1 12.0 1.0
O A:GLN136 4.3 16.6 1.0
CA A:GLN136 4.4 15.5 1.0
N A:GLN136 4.4 13.5 1.0
CA A:PRO138 4.4 11.6 1.0
N A:GLU205 4.4 11.7 1.0
O A:HOH364 4.4 14.9 1.0
CA A:GLU205 4.6 11.3 1.0
CA A:VAL135 4.8 13.5 1.0
CB A:LEU204 4.9 15.2 1.0
O A:ALA134 5.0 15.2 1.0
C A:CYS206 5.0 10.1 1.0
C A:LEU204 5.0 12.8 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: Wed Oct 28 18:40:44 2020

Last articles

Xe in 6AYK
Xe in 6QII
Xe in 6ASM
Xe in 5NSW
Xe in 6FY9
Xe in 5O1K
Xe in 5O27
Xe in 5M69
Xe in 5KPU
Xe in 5I63
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy