Zinc in PDB 5in3: Crystal Structure of Glucose-1-Phosphate Bound Nucleotidylated Human Galactose-1-Phosphate Uridylyltransferase

All present enzymatic activity of Crystal Structure of Glucose-1-Phosphate Bound Nucleotidylated Human Galactose-1-Phosphate Uridylyltransferase:
2.7.7.12;

The structure of Crystal Structure of Glucose-1-Phosphate Bound Nucleotidylated Human Galactose-1-Phosphate Uridylyltransferase, PDB code: 5in3 was solved by J.Kopec, T.Mccorvie, C.Tallant, S.Velupillai, L.Shrestha, F.Fitzpatrick, D.Patel, R.Chalk, N.Burgess-Brown, F.Von Delft, C.Arrowsmith, A.Edwards, C.Bountra, W.W.Yue, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.29 / 1.73
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	59.760, 107.990, 126.420, 90.00, 90.00, 90.00
R / Rfree (%)	19.8 / 22.8

The binding sites of Zinc atom in the Crystal Structure of Glucose-1-Phosphate Bound Nucleotidylated Human Galactose-1-Phosphate Uridylyltransferase (pdb code 5in3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Glucose-1-Phosphate Bound Nucleotidylated Human Galactose-1-Phosphate Uridylyltransferase, PDB code: 5in3:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Glucose-1-Phosphate Bound Nucleotidylated Human Galactose-1-Phosphate Uridylyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Crystal Structure of Glucose-1-Phosphate Bound Nucleotidylated Human Galactose-1-Phosphate Uridylyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:22.6 occ:0.54 ND1 B:HIS301 2.0 21.7 1.0 OE2 B:GLU202 2.0 27.1 1.0 NE2 B:HIS319 2.1 29.0 1.0 NE2 B:HIS321 2.1 23.6 1.0 OE1 B:GLU202 2.4 30.1 1.0 CD B:GLU202 2.5 28.1 1.0 CD2 B:HIS319 2.9 24.6 1.0 CE1 B:HIS301 2.9 28.0 1.0 CG B:HIS301 3.0 27.2 1.0 HD2 B:HIS319 3.0 29.5 1.0 CD2 B:HIS321 3.0 24.2 1.0 HB2 B:HIS301 3.0 36.3 1.0 HE1 B:HIS301 3.1 33.6 1.0 HD2 B:HIS321 3.1 29.0 1.0 CE1 B:HIS319 3.1 23.0 1.0 CE1 B:HIS321 3.2 27.1 1.0 HD21 B:LEU37 3.3 33.5 1.0 HE1 B:HIS321 3.4 32.6 1.0 CB B:HIS301 3.4 30.2 1.0 HE1 B:HIS319 3.4 27.6 1.0 HB3 B:HIS301 3.5 36.3 1.0 HE21 B:GLN38 3.5 31.2 1.0 CG B:GLU202 4.0 26.1 1.0 NE2 B:HIS301 4.1 26.3 1.0 HD23 B:LEU37 4.1 33.5 1.0 CD2 B:LEU37 4.1 27.9 1.0 CG B:HIS319 4.1 22.7 1.0 CD2 B:HIS301 4.1 23.4 1.0 ND1 B:HIS319 4.2 23.7 1.0 CG B:HIS321 4.2 24.7 1.0 ND1 B:HIS321 4.2 23.7 1.0 NE2 B:GLN38 4.2 26.0 1.0 HG3 B:GLU202 4.3 31.3 1.0 HG2 B:GLU202 4.4 31.3 1.0 HE22 B:GLN38 4.4 31.2 1.0 HG B:LEU37 4.4 32.9 1.0 HD11 B:LEU37 4.7 34.5 1.0 HB3 B:GLU202 4.7 29.8 1.0 HG22 B:ILE198 4.8 36.1 1.0 HD22 B:LEU37 4.8 33.5 1.0 CG B:LEU37 4.8 27.4 1.0 HE2 B:HIS301 4.8 31.6 1.0 CA B:HIS301 4.9 28.0 1.0 CB B:GLU202 4.9 24.9 1.0 O B:HOH551 4.9 25.2 1.0 HZ3 B:TRP316 4.9 34.1 1.0 HD1 B:HIS319 5.0 28.4 1.0 HD2 B:HIS301 5.0 28.1 1.0 HG21 B:ILE198 5.0 36.1 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Glucose-1-Phosphate Bound Nucleotidylated Human Galactose-1-Phosphate Uridylyltransferase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Crystal Structure of Glucose-1-Phosphate Bound Nucleotidylated Human Galactose-1-Phosphate Uridylyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:26.6 occ:0.67 ND1 A:HIS301 2.0 24.9 1.0 OE2 A:GLU202 2.0 24.7 1.0 NE2 A:HIS319 2.3 17.5 1.0 NE2 A:HIS321 2.3 22.9 1.0 OE1 A:GLU202 2.3 27.6 1.0 CD A:GLU202 2.4 27.0 1.0 CE1 A:HIS301 2.9 22.5 1.0 CG A:HIS301 3.0 19.7 1.0 CD2 A:HIS321 3.0 19.7 1.0 HD2 A:HIS321 3.1 23.6 1.0 HE1 A:HIS301 3.1 27.0 1.0 HB2 A:HIS301 3.1 23.6 1.0 CD2 A:HIS319 3.1 21.6 1.0 HD2 A:HIS319 3.2 25.9 1.0 HD21 A:LEU37 3.2 29.1 1.0 CE1 A:HIS319 3.3 22.1 1.0 CE1 A:HIS321 3.4 23.4 1.0 CB A:HIS301 3.4 19.7 1.0 HE21 A:GLN38 3.5 30.1 1.0 HB3 A:HIS301 3.5 23.6 1.0 HE1 A:HIS319 3.5 26.5 1.0 HE1 A:HIS321 3.7 28.1 1.0 CG A:GLU202 3.9 22.8 1.0 NE2 A:HIS301 4.0 21.6 1.0 CD2 A:LEU37 4.1 24.2 1.0 CD2 A:HIS301 4.1 21.6 1.0 HD23 A:LEU37 4.1 29.1 1.0 NE2 A:GLN38 4.2 25.0 1.0 HG3 A:GLU202 4.2 27.4 1.0 CG A:HIS321 4.3 22.1 1.0 CG A:HIS319 4.3 20.6 1.0 HG2 A:GLU202 4.3 27.4 1.0 ND1 A:HIS319 4.3 19.3 1.0 HE22 A:GLN38 4.3 30.1 1.0 ND1 A:HIS321 4.4 22.3 1.0 HG A:LEU37 4.4 27.3 1.0 HD11 A:LEU37 4.7 26.8 1.0 HB3 A:GLU202 4.7 28.3 1.0 HG22 A:ILE198 4.7 36.3 1.0 HD22 A:LEU37 4.8 29.1 1.0 O A:HOH583 4.8 23.2 1.0 CG A:LEU37 4.8 22.8 1.0 HE2 A:HIS301 4.8 25.9 1.0 HZ3 A:TRP316 4.9 32.5 1.0 CB A:GLU202 4.9 23.6 1.0 CA A:HIS301 4.9 15.3 1.0 HG21 A:ILE198 5.0 36.3 1.0 HD2 A:HIS301 5.0 26.0 1.0 HB2 A:GLU202 5.0 28.3 1.0

T.J.Mccorvie, J.Kopec, A.L.Pey, F.Fitzpatrick, D.Patel, R.Chalk, L.Shrestha, W.W.Yue. Molecular Basis of Classic Galactosemia From the Structure of Human Galactose 1-Phosphate Uridylyltransferase. Hum.Mol.Genet. V. 25 2234 2016.
ISSN: ESSN 1460-2083
PubMed: 27005423
DOI: 10.1093/HMG/DDW091