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Zinc in PDB 1hed: Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II

Enzymatic activity of Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II

All present enzymatic activity of Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II:
4.2.1.1;

Protein crystallography data

The structure of Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II, PDB code: 1hed was solved by S.K.Nair, D.W.Christianson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) N/A / 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 (%) n/a / n/a

Other elements in 1hed:

The structure of Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II also contains other interesting chemical elements:

Mercury (Hg) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II (pdb code 1hed). 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 Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II, PDB code: 1hed:

Zinc binding site 1 out of 1 in 1hed

Go back to Zinc Binding Sites List in 1hed
Zinc binding site 1 out of 1 in the Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structural Consequences of Hydrophilic Amino-Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn262

b:6.5
occ:1.00
 ND1 A:HIS119 2.0 3.2 1.0
NE2 A:HIS94 2.1 3.2 1.0
NE2 A:HIS96 2.1 3.4 1.0
O A:HOH342 2.1 8.5 1.0
CE1 A:HIS119 2.8 3.1 1.0
CD2 A:HIS94 3.0 3.4 1.0
CD2 A:HIS96 3.0 3.2 1.0
CE1 A:HIS96 3.2 3.2 1.0
CG A:HIS119 3.2 3.1 1.0
CE1 A:HIS94 3.2 3.1 1.0
CB A:HIS119 3.7 2.6 1.0
OG1 A:THR199 3.8 1.5 1.0
O A:HOH362 3.9 19.5 1.0
O A:HOH343 4.0 9.3 1.0
OE1 A:GLU106 4.0 3.2 1.0
NE2 A:HIS119 4.1 2.9 1.0
CG A:HIS96 4.2 3.1 1.0
CG A:HIS94 4.2 3.2 1.0
CD2 A:HIS119 4.2 3.0 1.0
O A:HOH344 4.3 22.6 1.0
ND1 A:HIS96 4.3 3.4 1.0
ND1 A:HIS94 4.3 3.2 1.0
CD A:GLU106 4.9 3.3 1.0

Reference:

S.K.Nair, D.W.Christianson. Structural Consequences of Hydrophilic Amino Acid Substitutions in the Hydrophobic Pocket of Human Carbonic Anhydrase II. Biochemistry V. 32 4506 1993.
ISSN: ISSN 0006-2960
PubMed: 8485129
DOI: 10.1021/BI00068A005
Page generated: Sun Oct 13 02:12:32 2024

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