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Zinc in PDB 4mhn: Crystal Structure of A Glutaminyl Cyclase From Ixodes Scapularis

Enzymatic activity of Crystal Structure of A Glutaminyl Cyclase From Ixodes Scapularis

All present enzymatic activity of Crystal Structure of A Glutaminyl Cyclase From Ixodes Scapularis:
2.3.2.5;

Protein crystallography data

The structure of Crystal Structure of A Glutaminyl Cyclase From Ixodes Scapularis, PDB code: 4mhn was solved by K.F.Huang, H.L.Hsu, A.H.J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.15
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.278, 71.379, 80.076, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 18.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of A Glutaminyl Cyclase From Ixodes Scapularis (pdb code 4mhn). 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 Crystal Structure of A Glutaminyl Cyclase From Ixodes Scapularis, PDB code: 4mhn:

Zinc binding site 1 out of 1 in 4mhn

Go back to Zinc Binding Sites List in 4mhn
Zinc binding site 1 out of 1 in the Crystal Structure of A Glutaminyl Cyclase From Ixodes Scapularis


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 A Glutaminyl Cyclase From Ixodes Scapularis within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn400

b:14.8
occ:1.00
OE2 A:GLU184 1.8 12.4 1.0
O A:HOH827 1.9 18.7 1.0
NE2 A:HIS322 2.0 11.6 1.0
OD2 A:ASP144 2.0 9.8 1.0
CD A:GLU184 2.8 11.2 1.0
CG A:ASP144 2.8 9.0 1.0
CD2 A:HIS322 2.8 10.7 1.0
OD1 A:ASP144 2.9 9.5 1.0
OE1 A:GLU184 3.0 12.8 1.0
CE1 A:HIS322 3.1 11.8 1.0
O A:HOH644 3.7 16.5 1.0
O A:HOH635 3.7 23.7 1.0
O A:HOH540 3.8 10.7 1.0
NE1 A:TRP321 4.0 10.6 1.0
CG A:HIS322 4.1 10.5 1.0
ND1 A:HIS322 4.1 11.4 1.0
CG A:GLU184 4.2 10.8 1.0
CB A:ASP144 4.2 9.0 1.0
OE1 A:GLU183 4.4 15.3 1.0
O A:HOH517 4.6 9.7 1.0
CE2 A:TRP321 4.6 10.2 1.0
CD1 A:TRP321 4.7 10.6 1.0
NE2 A:HIS128 4.7 10.1 1.0
CD2 A:LEU239 4.8 9.3 1.0
CZ2 A:TRP321 4.8 11.4 1.0
CE1 A:HIS128 4.9 9.4 1.0
CB A:LEU132 4.9 9.7 1.0
O A:ASP144 5.0 9.0 1.0

Reference:

K.F.Huang, H.L.Hsu, S.Karim, A.H.J.Wang. Structural and Functional Analyses of A Glutaminyl Cyclase From Ixodes Scapularis Reveal Metal-Independent Catalysis and Inhibitor Binding. Acta Crystallogr.,Sect.D V. 70 789 2014.
ISSN: ISSN 0907-4449
DOI: 10.1107/S1399004713033488
Page generated: Sun Oct 27 02:28:08 2024

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