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Manganese in PDB 7d2d: Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Mn Ion Bound to the Active Site

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

All present enzymatic activity of Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Mn 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 Mn Ion Bound to the Active Site, PDB code: 7d2d 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) 21.90 / 1.80
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 55.035, 71.582, 80.145, 90, 90, 90
R / Rfree (%) 17.3 / 21.5

Manganese Binding Sites:

The binding sites of Manganese atom in the Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Mn Ion Bound to the Active Site (pdb code 7d2d). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Mn Ion Bound to the Active Site, PDB code: 7d2d:

Manganese binding site 1 out of 1 in 7d2d

Go back to Manganese Binding Sites List in 7d2d
Manganese binding site 1 out of 1 in the Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Mn Ion Bound to the Active Site


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Crystal Structure of Ixodes Scapularis Glutaminyl Cyclase with A Mn Ion Bound to the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mn400

b:13.5
occ:1.00
 O A:HOH731 1.8 18.7 1.0
OE2 A:GLU184 1.9 16.8 1.0
OD2 A:ASP144 2.0 14.2 1.0
NE2 A:HIS322 2.0 17.5 1.0
CD A:GLU184 2.7 16.6 1.0
CG A:ASP144 2.8 13.7 1.0
OE1 A:GLU184 2.9 16.8 1.0
OD1 A:ASP144 2.9 13.4 1.0
CD2 A:HIS322 2.9 16.8 1.0
CE1 A:HIS322 3.1 18.1 1.0
O A:HOH560 3.7 28.0 1.0
O A:HOH536 3.8 14.6 1.0
NE1 A:TRP321 3.9 15.9 1.0
O A:HOH746 4.1 37.9 1.0
CG A:HIS322 4.1 17.4 1.0
ND1 A:HIS322 4.2 17.2 1.0
CG A:GLU184 4.2 15.9 1.0
CB A:ASP144 4.2 13.1 1.0
OE1 A:GLU183 4.4 18.2 1.0
CE2 A:TRP321 4.5 16.8 1.0
O A:HOH589 4.5 14.1 1.0
CD1 A:TRP321 4.7 16.8 1.0
CD2 A:LEU239 4.7 11.7 1.0
NE2 A:HIS128 4.7 13.5 1.0
CZ2 A:TRP321 4.7 16.9 1.0
CB A:LEU132 4.9 14.6 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 Aug 16 22:30:56 2025

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