Atomistry » Zinc » PDB 6gni-6h0s » 6gqd
Atomistry »
  Zinc »
    PDB 6gni-6h0s »
      6gqd »

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: Mon Oct 28 21:59:02 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy