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Iron in PDB 7d2i: Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Fe Ion Bound to the Active Site

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

All present enzymatic activity of Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Fe 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 Fe Ion Bound to the Active Site, PDB code: 7d2i 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) 26.80 / 1.85
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.629, 71.478, 80.926, 90, 90, 90
R / Rfree (%) 17.8 / 22.8

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Fe Ion Bound to the Active Site (pdb code 7d2i). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Fe Ion Bound to the Active Site, PDB code: 7d2i:

Iron binding site 1 out of 1 in 7d2i

Go back to Iron Binding Sites List in 7d2i
Iron binding site 1 out of 1 in the Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Fe Ion Bound to the Active Site


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Fe Ion Bound to the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:24.7
occ:1.00
 OD2 A:ASP144 2.0 16.7 1.0
OE2 A:GLU184 2.1 16.0 1.0
NE2 A:HIS322 2.1 17.9 1.0
O A:HOH501 2.4 28.9 1.0
O4 A:SO4402 2.6 66.8 1.0
CG A:ASP144 2.8 15.6 1.0
CD A:GLU184 2.9 16.2 1.0
OD1 A:ASP144 2.9 15.4 1.0
OE1 A:GLU184 2.9 17.5 1.0
CD2 A:HIS322 3.0 17.4 1.0
CE1 A:HIS322 3.2 18.6 1.0
S A:SO4402 3.6 76.5 1.0
NE1 A:TRP321 3.8 18.5 1.0
O3 A:SO4402 3.9 66.5 1.0
O2 A:SO4402 4.0 67.6 1.0
O A:HOH571 4.1 18.1 1.0
CG A:HIS322 4.2 18.3 1.0
ND1 A:HIS322 4.2 17.2 1.0
CB A:ASP144 4.3 15.3 1.0
CG A:GLU184 4.3 16.1 1.0
OE1 A:GLU183 4.4 21.4 1.0
CD2 A:LEU239 4.6 12.9 1.0
CD1 A:TRP321 4.6 18.1 1.0
CE2 A:TRP321 4.6 18.4 1.0
NE2 A:HIS128 4.8 15.0 1.0
O A:HOH546 4.8 15.2 1.0
CZ2 A:TRP321 4.9 18.9 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: Wed Aug 6 21:31:01 2025

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