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Zinc in PDB 5cjo: Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (Ide) in Complex with Insulin

Enzymatic activity of Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (Ide) in Complex with Insulin

All present enzymatic activity of Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (Ide) in Complex with Insulin:
3.4.24.56;

Protein crystallography data

The structure of Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (Ide) in Complex with Insulin, PDB code: 5cjo was solved by W.G.Liang, L.Bailey, W.J.Tang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.45 / 3.29
Space group P 2 21 21
Cell size a, b, c (Å), α, β, γ (°) 75.689, 109.218, 263.405, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / 24.5

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (Ide) in Complex with Insulin (pdb code 5cjo). 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 Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (Ide) in Complex with Insulin, PDB code: 5cjo:

Zinc binding site 1 out of 1 in 5cjo

Go back to Zinc Binding Sites List in 5cjo
Zinc binding site 1 out of 1 in the Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (Ide) in Complex with Insulin


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure Analysis of Elbow-Engineered-Fab-Bound Human Insulin Degrading Enzyme (Ide) in Complex with Insulin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn2002

b:67.8
occ:1.00
 OE1 A:GLU189 2.1 74.0 1.0
NE2 A:HIS108 2.1 58.4 1.0
NE2 A:HIS112 2.2 50.4 1.0
CD A:GLU189 2.9 72.1 1.0
OE2 A:GLU189 3.1 67.9 1.0
CE1 A:HIS112 3.1 51.7 1.0
CD2 A:HIS108 3.1 67.9 1.0
CE1 A:HIS108 3.1 63.9 1.0
CD2 A:HIS112 3.2 70.5 1.0
CB a:TYR14 3.3 0.2 1.0
CD2 a:TYR14 3.4 0.7 1.0
CG a:TYR14 3.6 0.2 1.0
N a:GLN15 4.2 0.9 1.0
ND1 A:HIS108 4.2 68.3 1.0
ND1 A:HIS112 4.2 58.4 1.0
CG A:HIS108 4.3 71.1 1.0
NE2 A:GLN111 4.3 58.0 1.0
CG A:HIS112 4.3 67.3 1.0
CG A:GLU189 4.4 73.5 1.0
CB a:GLN15 4.4 0.1 1.0
CE2 a:TYR14 4.4 0.6 1.0
C a:TYR14 4.5 0.6 1.0
CA a:TYR14 4.5 0.9 1.0
OE1 A:GLN111 4.7 63.4 1.0
CD A:GLN111 4.7 54.7 1.0
CA a:GLN15 4.8 0.1 1.0
CE1 A:TYR831 4.8 67.9 1.0
CD1 a:TYR14 4.9 0.3 1.0
CB A:GLU189 4.9 73.0 1.0

Reference:

L.J.Bailey, K.M.Sheehy, P.K.Dominik, W.G.Liang, H.Rui, M.Clark, M.Jaskolowski, Y.Kim, D.Deneka, W.J.Tang, A.A.Kossiakoff. Locking the Elbow: Improved Antibody Fab Fragments As Chaperones For Structure Determination. J. Mol. Biol. 2017.
ISSN: ESSN 1089-8638
PubMed: 29273204
DOI: 10.1016/J.JMB.2017.12.012
Page generated: Wed Dec 16 06:07:12 2020

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