Zinc in PDB 6gqd: Structure of Human Galactose-1-Phosphate Uridylyltransferase (Galt), with Crystallization Epitope Mutations A21Y:A22T:T23P:R25L

Enzymatic activity of Structure of Human Galactose-1-Phosphate Uridylyltransferase (Galt), with Crystallization Epitope Mutations A21Y:A22T:T23P:R25L

All present enzymatic activity of Structure of Human Galactose-1-Phosphate Uridylyltransferase (Galt), with Crystallization Epitope Mutations A21Y:A22T:T23P:R25L:
2.7.7.12;

Protein crystallography data

The structure of Structure of Human Galactose-1-Phosphate Uridylyltransferase (Galt), with Crystallization Epitope Mutations A21Y:A22T:T23P:R25L, PDB code: 6gqd was solved by M.Fairhead, C.Strain-Damerell, J.Kopec, G.A.Bezerra, M.Zhang, N.Burgess-Brown, F.Von Delft, C.Arrowsmith, A.Edwards, C.Bountra, W.W.Yue, Structural Genomics Consortium (Sgc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 58.09 / 1.52
Space group P 21 21 2
Cell size a, b, c (Å), α, β, γ (°) 72.647, 96.748, 55.426, 90.00, 90.00, 90.00
R / Rfree (%) 16.2 / 18.8

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Human Galactose-1-Phosphate Uridylyltransferase (Galt), with Crystallization Epitope Mutations A21Y:A22T:T23P:R25L (pdb code 6gqd). 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 Human Galactose-1-Phosphate Uridylyltransferase (Galt), with Crystallization Epitope Mutations A21Y:A22T:T23P:R25L, PDB code: 6gqd:

Zinc binding site 1 out of 1 in 6gqd

Go back to Zinc Binding Sites List in 6gqd
Zinc binding site 1 out of 1 in the Structure of Human Galactose-1-Phosphate Uridylyltransferase (Galt), with Crystallization Epitope Mutations A21Y:A22T:T23P:R25L


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human Galactose-1-Phosphate Uridylyltransferase (Galt), with Crystallization Epitope Mutations A21Y:A22T:T23P:R25L within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn401

b:16.2
occ:0.64
 OE2 A:GLU202 1.9 21.4 1.0
ND1 A:HIS301 2.1 14.2 1.0
NE2 A:HIS319 2.1 14.8 1.0
NE2 A:HIS321 2.2 15.0 1.0
OE1 A:GLU202 2.5 19.8 1.0
CD A:GLU202 2.5 19.4 1.0
CE1 A:HIS301 3.0 16.0 1.0
CD2 A:HIS319 3.0 16.4 1.0
CE1 A:HIS321 3.1 14.4 1.0
HB2 A:HIS301 3.1 15.9 1.0
HE1 A:HIS301 3.1 19.2 1.0
CE1 A:HIS319 3.2 15.5 1.0
CG A:HIS301 3.2 14.1 1.0
HD2 A:HIS319 3.2 19.6 1.0
CD2 A:HIS321 3.2 15.4 1.0
HE1 A:HIS321 3.2 17.3 1.0
HE1 A:HIS319 3.4 18.6 1.0
HD2 A:HIS321 3.4 18.4 1.0
HD21 A:LEU37 3.5 29.2 1.0
CB A:HIS301 3.5 13.3 1.0
HE21 A:GLN38 3.7 27.1 1.0
HB3 A:HIS301 3.7 15.9 1.0
CG A:GLU202 4.0 16.8 1.0
NE2 A:HIS301 4.1 15.2 1.0
CG A:HIS319 4.2 14.0 1.0
ND1 A:HIS319 4.2 14.9 1.0
ND1 A:HIS321 4.2 14.0 1.0
CD2 A:HIS301 4.2 15.8 1.0
HD23 A:LEU37 4.3 29.2 1.0
CD2 A:LEU37 4.3 24.3 1.0
HG3 A:GLU202 4.3 20.2 1.0
CG A:HIS321 4.3 16.5 1.0
HG2 A:GLU202 4.3 20.2 1.0
NE2 A:GLN38 4.4 22.6 1.0
HG A:LEU37 4.5 31.3 1.0
HE22 A:GLN38 4.6 27.1 1.0
HD11 A:LEU37 4.7 24.7 1.0
HG22 A:ILE198 4.9 26.4 1.0
O A:HOH610 4.9 14.6 1.0
HB3 A:GLU202 4.9 20.9 1.0
HE2 A:HIS301 4.9 18.3 1.0
CG A:LEU37 4.9 26.1 1.0
HD1 A:HIS321 5.0 16.8 1.0

Reference:

M.Fairhead, C.Strain-Damerell, J.Kopec, G.A.Bezerra, M.Zhang, N.Burgess-Brown, F.Von Delft, C.Arrowsmith, A.Edwards, C.Bountra, W.W.Yue. Structure of Human Galactose-1-Phosphate Uridylyltransferase (Galt), with Crystallization Epitope Mutations A21Y:A22T:T23P:R25L To Be Published.
Page generated: Wed Dec 16 11:53:08 2020

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