Atomistry » Zinc » PDB 2z56-2zeo » 2zed
Atomistry »
  Zinc »
    PDB 2z56-2zeo »
      2zed »

Zinc in PDB 2zed: Crystal Structure of the Human Glutaminyl Cyclase Mutant S160A at 1.7 Angstrom Resolution

Enzymatic activity of Crystal Structure of the Human Glutaminyl Cyclase Mutant S160A at 1.7 Angstrom Resolution

All present enzymatic activity of Crystal Structure of the Human Glutaminyl Cyclase Mutant S160A at 1.7 Angstrom Resolution:
2.3.2.5;

Protein crystallography data

The structure of Crystal Structure of the Human Glutaminyl Cyclase Mutant S160A at 1.7 Angstrom Resolution, PDB code: 2zed was solved by K.F.Huang, Y.R.Wang, E.C.Chang, T.L.Chou, A.H.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.70
Space group H 3 2
Cell size a, b, c (Å), α, β, γ (°) 118.926, 118.926, 332.499, 90.00, 90.00, 120.00
R / Rfree (%) 18 / 21.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of the Human Glutaminyl Cyclase Mutant S160A at 1.7 Angstrom Resolution (pdb code 2zed). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Human Glutaminyl Cyclase Mutant S160A at 1.7 Angstrom Resolution, PDB code: 2zed:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2zed

Go back to Zinc Binding Sites List in 2zed
Zinc binding site 1 out of 2 in the Crystal Structure of the Human Glutaminyl Cyclase Mutant S160A at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of the Human Glutaminyl Cyclase Mutant S160A at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn391

b:20.6
occ:1.00
OE2 A:GLU202 2.0 19.7 1.0
OD2 A:ASP159 2.0 18.5 1.0
NE2 A:HIS330 2.1 19.4 1.0
O A:HOH401 2.1 25.6 1.0
CD A:GLU202 2.7 18.7 1.0
CG A:ASP159 2.8 20.9 1.0
OD1 A:ASP159 2.9 20.9 1.0
OE1 A:GLU202 2.9 18.6 1.0
CD2 A:HIS330 3.0 20.1 1.0
CE1 A:HIS330 3.1 19.3 1.0
O A:HOH538 4.0 20.5 1.0
CG A:GLU202 4.2 18.7 1.0
CG A:HIS330 4.2 18.5 1.0
CB A:ASP159 4.2 18.7 1.0
ND1 A:HIS330 4.2 18.9 1.0
O A:HOH809 4.3 28.4 1.0
NE1 A:TRP329 4.3 17.4 1.0
OE1 A:GLU201 4.3 20.3 1.0
O A:HOH534 4.5 18.7 1.0
CD2 A:LEU249 4.6 18.4 1.0
NE2 A:HIS140 4.6 17.4 1.0
CD1 A:TRP329 4.7 19.1 1.0
CE1 A:HIS140 4.8 17.8 1.0

Zinc binding site 2 out of 2 in 2zed

Go back to Zinc Binding Sites List in 2zed
Zinc binding site 2 out of 2 in the Crystal Structure of the Human Glutaminyl Cyclase Mutant S160A at 1.7 Angstrom Resolution


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of the Human Glutaminyl Cyclase Mutant S160A at 1.7 Angstrom Resolution within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn392

b:23.5
occ:1.00
NE2 B:HIS330 1.9 22.2 1.0
OE2 B:GLU202 2.0 23.3 1.0
OD2 B:ASP159 2.1 21.5 1.0
O B:HOH402 2.1 31.8 1.0
CD B:GLU202 2.7 22.6 1.0
CG B:ASP159 2.8 21.5 1.0
CD2 B:HIS330 2.9 23.4 1.0
OE1 B:GLU202 2.9 22.2 1.0
CE1 B:HIS330 3.0 24.5 1.0
OD1 B:ASP159 3.0 22.5 1.0
O B:HOH468 4.0 19.0 1.0
CG B:HIS330 4.0 24.6 1.0
ND1 B:HIS330 4.0 24.4 1.0
NE1 B:TRP329 4.1 27.3 1.0
CG B:GLU202 4.2 20.9 1.0
CB B:ASP159 4.3 20.7 1.0
OE1 B:GLU201 4.3 23.7 1.0
O B:HOH464 4.5 22.6 1.0
O B:HOH1191 4.5 49.9 1.0
CD1 B:TRP329 4.7 28.4 1.0
NE2 B:HIS140 4.8 20.6 1.0
CD2 B:LEU249 4.8 23.1 1.0
CE2 B:TRP329 4.8 27.4 1.0
CD B:LYS144 4.9 22.7 1.0
CE1 B:HIS140 5.0 19.9 1.0

Reference:

K.F.Huang, Y.R.Wang, E.C.Chang, T.L.Chou, A.H.Wang. A Conserved Hydrogen-Bond Network in the Catalytic Centre of Animal Glutaminyl Cyclases Is Critical For Catalysis. Biochem.J. V. 411 181 2008.
ISSN: ISSN 0264-6021
PubMed: 18072935
DOI: 10.1042/BJ20071073
Page generated: Thu Oct 24 10:45:06 2024

Last articles

Mn in 5BKC
Mn in 5BKD
Mn in 5BKB
Mn in 5B4C
Mn in 5B32
Mn in 5B1L
Mn in 5B49
Mn in 5B31
Mn in 5B2J
Mn in 5B2I
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy