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Cadmium in PDB 7d2j: Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Cd Ion Bound to the Active Site

Enzymatic activity of Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Cd Ion Bound to the Active Site

All present enzymatic activity of Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Cd Ion Bound to the Active Site:
2.3.2.5;

Protein crystallography data

The structure of Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Cd Ion Bound to the Active Site, PDB code: 7d2j was solved by K.-F.Huang, J.-S.Huang, M.-L.Wu, W.-L.Hsieh, A.H.-J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 22.98 / 1.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.127, 71.936, 80.186, 90, 90, 90
R / Rfree (%) 17 / 19.7

Cadmium Binding Sites:

The binding sites of Cadmium atom in the Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Cd Ion Bound to the Active Site (pdb code 7d2j). This binding sites where shown within 5.0 Angstroms radius around Cadmium atom.
In total only one binding site of Cadmium was determined in the Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Cd Ion Bound to the Active Site, PDB code: 7d2j:

Cadmium binding site 1 out of 1 in 7d2j

Go back to Cadmium Binding Sites List in 7d2j
Cadmium binding site 1 out of 1 in the Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Cd Ion Bound to the Active Site


Mono view


Stereo pair view

A full contact list of Cadmium with other atoms in the Cd binding site number 1 of Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Cd Ion Bound to the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cd401

b:12.2
occ:1.00
 OE2 A:GLU184 2.2 12.2 1.0
NE2 A:HIS322 2.2 12.2 1.0
O3 A:BCT402 2.3 19.2 1.0
OD2 A:ASP144 2.4 10.7 1.0
O2 A:BCT402 2.5 17.1 1.0
OD1 A:ASP144 2.6 10.2 1.0
CG A:ASP144 2.8 10.3 1.0
C A:BCT402 2.8 20.1 1.0
OE1 A:GLU184 2.8 13.1 1.0
CD A:GLU184 2.8 12.5 1.0
CD2 A:HIS322 3.2 12.9 1.0
CE1 A:HIS322 3.2 12.4 1.0
NE1 A:TRP321 4.1 13.0 1.0
O1 A:BCT402 4.1 24.1 1.0
O A:HOH564 4.1 12.2 1.0
OE1 A:GLU183 4.2 14.3 1.0
CB A:ASP144 4.3 10.4 1.0
CG A:GLU184 4.3 12.1 1.0
CG A:HIS322 4.3 12.5 1.0
ND1 A:HIS322 4.3 13.3 1.0
NE2 A:HIS128 4.4 12.2 1.0
O A:HOH786 4.6 31.4 1.0
CE1 A:HIS128 4.7 12.3 1.0
CE2 A:TRP321 4.7 13.4 1.0
CD2 A:LEU239 4.7 11.0 1.0
CZ2 A:TRP321 4.8 13.4 1.0
O A:HOH577 4.8 11.9 1.0
CD1 A:TRP321 4.9 12.7 1.0
O A:HOH542 4.9 16.8 1.0

Reference:

K.F.Huang, J.S.Huang, M.L.Wu, W.L.Hsieh, K.C.Hsu, H.L.Hsu, T.P.Ko, A.H-J Wang. A Unique Carboxylic-Acid Hydrogen-Bond Network (Cahbn) Confers Glutaminyl Cyclase Activity on M28 Family Enzymes. J.Mol.Biol. 66960 2021.
ISSN: ESSN 1089-8638
PubMed: 33774034
DOI: 10.1016/J.JMB.2021.166960
Page generated: Sat Apr 17 14:38:38 2021

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