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Zinc in PDB 5t72: Human Carboanhydrase F131C_C206S Double Mutant in Complex with 2

Enzymatic activity of Human Carboanhydrase F131C_C206S Double Mutant in Complex with 2

All present enzymatic activity of Human Carboanhydrase F131C_C206S Double Mutant in Complex with 2:
4.2.1.1;

Protein crystallography data

The structure of Human Carboanhydrase F131C_C206S Double Mutant in Complex with 2, PDB code: 5t72 was solved by K.H.Dubay, K.Iwan, L.Osorio-Planes, P.Geissler, M.Groll, D.Trauner, J.Broichhagen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 15.00 / 1.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.350, 41.190, 72.230, 90.00, 104.09, 90.00
R / Rfree (%) 14.8 / 16.6

Other elements in 5t72:

The structure of Human Carboanhydrase F131C_C206S Double Mutant in Complex with 2 also contains other interesting chemical elements:

Mercury (Hg) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Carboanhydrase F131C_C206S Double Mutant in Complex with 2 (pdb code 5t72). 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 Carboanhydrase F131C_C206S Double Mutant in Complex with 2, PDB code: 5t72:

Zinc binding site 1 out of 1 in 5t72

Go back to Zinc Binding Sites List in 5t72
Zinc binding site 1 out of 1 in the Human Carboanhydrase F131C_C206S Double Mutant in Complex with 2


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Carboanhydrase F131C_C206S Double Mutant in Complex with 2 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:5.5
occ:1.00
NE2 A:HIS96 2.1 6.0 1.0
ND1 A:HIS119 2.1 4.8 1.0
NE2 A:HIS94 2.1 5.9 1.0
N8 A:4WA303 2.1 4.8 0.5
N8 A:4WA303 2.1 7.3 0.5
CE1 A:HIS119 2.9 4.8 1.0
O10 A:4WA303 2.9 5.0 0.5
CD2 A:HIS94 3.0 6.1 1.0
CD2 A:HIS96 3.0 5.9 1.0
S18 A:4WA303 3.0 5.1 0.5
O10 A:4WA303 3.1 7.8 0.5
CE1 A:HIS96 3.1 6.5 1.0
CE1 A:HIS94 3.1 6.0 1.0
S18 A:4WA303 3.1 8.2 0.5
CG A:HIS119 3.1 4.7 1.0
CB A:HIS119 3.6 4.8 1.0
OG1 A:THR198 3.9 6.1 1.0
OE1 A:GLU106 4.0 6.8 1.0
O9 A:4WA303 4.0 5.2 0.5
NE2 A:HIS119 4.1 4.9 1.0
C4 A:4WA303 4.1 6.6 0.5
CG A:HIS94 4.1 5.9 1.0
ND1 A:HIS96 4.2 6.5 1.0
CG A:HIS96 4.2 5.8 1.0
O9 A:4WA303 4.2 7.9 0.5
C4 A:4WA303 4.2 9.8 0.5
ND1 A:HIS94 4.2 5.8 1.0
CD2 A:HIS119 4.2 4.8 1.0
C3 A:TRS304 4.5 16.3 1.0
N A:TRS304 4.6 17.3 1.0
C5 A:4WA303 4.9 10.9 0.5
CD A:GLU106 4.9 6.8 1.0
C5 A:4WA303 4.9 7.7 0.5
C3 A:4WA303 4.9 7.5 0.5

Reference:

K.H.Dubay, K.Iwan, L.Osorio-Planes, P.L.Geissler, M.Groll, D.Trauner, J.Broichhagen. A Predictive Approach For the Optical Control of Carbonic Anhydrase II Activity. Acs Chem. Biol. V. 13 793 2018.
ISSN: ESSN 1554-8937
PubMed: 29357237
DOI: 10.1021/ACSCHEMBIO.7B00862
Page generated: Wed Dec 16 10:53:52 2020

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