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Zinc in PDB 6ypi: Structure of the Engineered Metallo-Diels-Alderase DA7 W16G,K58Q,L77R, T78R

Protein crystallography data

The structure of Structure of the Engineered Metallo-Diels-Alderase DA7 W16G,K58Q,L77R, T78R, PDB code: 6ypi was solved by S.Basler, T.Mori, D.Hilvert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 40.67 / 1.48
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 62.237, 35.015, 43.229, 90, 109.81, 90
R / Rfree (%) 20.7 / 23

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of the Engineered Metallo-Diels-Alderase DA7 W16G,K58Q,L77R, T78R (pdb code 6ypi). 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 Structure of the Engineered Metallo-Diels-Alderase DA7 W16G,K58Q,L77R, T78R, PDB code: 6ypi:

Zinc binding site 1 out of 1 in 6ypi

Go back to Zinc Binding Sites List in 6ypi
Zinc binding site 1 out of 1 in the Structure of the Engineered Metallo-Diels-Alderase DA7 W16G,K58Q,L77R, T78R


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of the Engineered Metallo-Diels-Alderase DA7 W16G,K58Q,L77R, T78R within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn101

b:18.0
occ:0.68
O2 A:BEZ104 1.9 25.8 1.0
NE2 A:HIS61 2.0 18.7 1.0
NE2 A:HIS65 2.0 20.1 1.0
SG A:CYS35 2.2 24.1 1.0
CE1 A:HIS61 2.9 28.0 1.0
CE1 A:HIS65 2.9 20.6 1.0
C A:BEZ104 3.0 36.7 1.0
CD2 A:HIS61 3.0 20.6 1.0
CD2 A:HIS65 3.1 23.8 1.0
CB A:CYS35 3.1 23.2 1.0
O1 A:BEZ104 3.3 38.5 1.0
CA A:CYS35 3.8 22.2 1.0
ND1 A:HIS61 4.0 26.2 1.0
ND1 A:HIS65 4.1 20.6 1.0
CG A:HIS61 4.1 19.8 1.0
CG A:HIS65 4.2 19.1 1.0
C1 A:BEZ104 4.3 28.8 1.0
C A:CYS35 4.6 26.4 1.0
O A:CYS35 4.7 24.0 1.0
C2 A:BEZ104 4.7 30.6 1.0
CG2 A:VAL39 4.8 39.8 1.0
N A:CYS35 4.9 24.3 1.0

Reference:

S.Basler, S.Studer, Y.Zou, T.Mori, Y.Ota, A.Camus, H.A.Bunzel, R.C.Helgeson, K.N.Houk, G.Jimenez-Oses, D.Hilvert. Catalysis of A Hetero-Diels-Alder Reaction By A De Novo Metalloenzyme To Be Published.
Page generated: Tue Oct 29 15:14:07 2024

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