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Zinc in PDB 6t4p: Human Carbonic Anhydrase II Bound By Napthalene-1-Sulfonamide

Enzymatic activity of Human Carbonic Anhydrase II Bound By Napthalene-1-Sulfonamide

All present enzymatic activity of Human Carbonic Anhydrase II Bound By Napthalene-1-Sulfonamide:
4.2.1.1;

Protein crystallography data

The structure of Human Carbonic Anhydrase II Bound By Napthalene-1-Sulfonamide, PDB code: 6t4p was solved by A.Smirnov, E.Manakova, S.Grazulis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 26.57 / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 42.072, 41.159, 71.704, 90.00, 104.08, 90.00
R / Rfree (%) 16.2 / 19.9

Other elements in 6t4p:

The structure of Human Carbonic Anhydrase II Bound By Napthalene-1-Sulfonamide also contains other interesting chemical elements:

Sodium (Na) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Human Carbonic Anhydrase II Bound By Napthalene-1-Sulfonamide (pdb code 6t4p). 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 Carbonic Anhydrase II Bound By Napthalene-1-Sulfonamide, PDB code: 6t4p:

Zinc binding site 1 out of 1 in 6t4p

Go back to Zinc Binding Sites List in 6t4p
Zinc binding site 1 out of 1 in the Human Carbonic Anhydrase II Bound By Napthalene-1-Sulfonamide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Human Carbonic Anhydrase II Bound By Napthalene-1-Sulfonamide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:7.2
occ:1.00
NE2 A:HIS94 2.0 5.8 1.0
N10 A:MHK305 2.0 8.4 1.0
ND1 A:HIS119 2.0 5.0 1.0
NE2 A:HIS96 2.0 7.6 1.0
CD2 A:HIS94 2.9 6.0 1.0
CE1 A:HIS119 3.0 5.3 1.0
CD2 A:HIS96 3.0 7.6 1.0
S7 A:MHK305 3.0 9.7 1.0
CE1 A:HIS94 3.1 6.2 1.0
O9 A:MHK305 3.1 8.8 1.0
CG A:HIS119 3.1 4.8 1.0
CE1 A:HIS96 3.1 7.8 1.0
CB A:HIS119 3.5 4.9 1.0
OE1 A:GLU106 3.9 7.5 1.0
OG1 A:THR199 3.9 6.9 1.0
C5 A:MHK305 4.0 14.1 1.0
C4 A:MHK305 4.1 11.6 1.0
CG A:HIS94 4.1 6.3 1.0
NE2 A:HIS119 4.1 5.1 1.0
ND1 A:HIS94 4.1 6.1 1.0
CG A:HIS96 4.1 7.4 1.0
ND1 A:HIS96 4.2 7.6 1.0
CD2 A:HIS119 4.2 4.9 1.0
O8 A:MHK305 4.2 9.3 1.0
CD A:GLU106 4.8 7.3 1.0
CA A:HIS119 5.0 5.6 1.0

Reference:

V.Dudutiene, A.Zubriene, V.Kairys, A.Smirnov, J.Smirnoviene, J.Leitans, A.Kazaks, K.Tars, L.Manakova, S.Grazulis, D.Matulis. Isoform-Selective Enzyme Inhibitors By Exploring Pocket Size According to the Lock-and-Key Principle. Biophys.J. V. 119 1513 2020.
ISSN: ESSN 1542-0086
PubMed: 32971003
DOI: 10.1016/J.BPJ.2020.08.037
Page generated: Wed Dec 16 12:51:21 2020

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