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Mercury in PDB 2cbc: Structure of Native and Apo Carbonic Anhydrase II and Some of Its Anion-Ligand Complexes

Enzymatic activity of Structure of Native and Apo Carbonic Anhydrase II and Some of Its Anion-Ligand Complexes

All present enzymatic activity of Structure of Native and Apo Carbonic Anhydrase II and Some of Its Anion-Ligand Complexes:
4.2.1.1;

Protein crystallography data

The structure of Structure of Native and Apo Carbonic Anhydrase II and Some of Its Anion-Ligand Complexes, PDB code: 2cbc was solved by K.Hakansson, M.Carlsson, L.A.Svensson, A.Liljas, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 1.88
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 (%) n/a / n/a

Other elements in 2cbc:

The structure of Structure of Native and Apo Carbonic Anhydrase II and Some of Its Anion-Ligand Complexes also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Mercury Binding Sites:

The binding sites of Mercury atom in the Structure of Native and Apo Carbonic Anhydrase II and Some of Its Anion-Ligand Complexes (pdb code 2cbc). 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 Structure of Native and Apo Carbonic Anhydrase II and Some of Its Anion-Ligand Complexes, PDB code: 2cbc:

Mercury binding site 1 out of 1 in 2cbc

Go back to Mercury Binding Sites List in 2cbc
Mercury binding site 1 out of 1 in the Structure of Native and Apo Carbonic Anhydrase II and Some of Its Anion-Ligand Complexes


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structure of Native and Apo Carbonic Anhydrase II and Some of Its Anion-Ligand Complexes within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Hg362

b:17.0
occ:1.00
O A:HOH365 2.5 39.6 1.0
SG A:CYS206 2.7 28.8 1.0
O A:HOH448 2.8 39.8 1.0
O A:GLN137 3.1 12.2 1.0
CB A:CYS206 3.2 14.8 1.0
C A:GLN137 3.4 12.8 1.0
CA A:CYS206 3.5 9.9 1.0
N A:GLN137 3.6 15.1 1.0
O A:GLU205 3.6 8.7 1.0
N A:CYS206 3.7 8.6 1.0
C A:GLU205 3.7 9.1 1.0
O A:VAL135 3.7 17.8 1.0
C A:GLN136 3.9 16.4 1.0
O A:HOH331 4.0 18.2 1.0
N A:PRO138 4.0 11.6 1.0
CA A:GLN137 4.0 13.7 1.0
C A:VAL135 4.1 16.0 1.0
CA A:PRO138 4.2 10.9 1.0
N A:GLU205 4.3 8.0 1.0
CA A:GLN136 4.4 15.8 1.0
N A:GLN136 4.5 15.4 1.0
O A:GLN136 4.5 17.1 1.0
CA A:GLU205 4.6 7.8 1.0
CB A:LEU204 4.9 10.9 1.0
O A:HOH443 4.9 73.4 1.0
CA A:VAL135 4.9 14.8 1.0
C A:LEU204 4.9 8.7 1.0
C A:CYS206 5.0 8.5 1.0
CD A:PRO138 5.0 11.7 1.0

Reference:

K.Hakansson, M.Carlsson, L.A.Svensson, A.Liljas. Structure of Native and Apo Carbonic Anhydrase II and Structure of Some of Its Anion-Ligand Complexes. J.Mol.Biol. V. 227 1192 1992.
ISSN: ISSN 0022-2836
PubMed: 1433293
DOI: 10.1016/0022-2836(92)90531-N
Page generated: Wed Oct 28 18:41:18 2020

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