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Zinc in PDB 1yj6: Crystal Structure of Human Glutathione S-Transferase M1A-1A Complexed with Glutathionyl-Zinc-Trihydroxide

Enzymatic activity of Crystal Structure of Human Glutathione S-Transferase M1A-1A Complexed with Glutathionyl-Zinc-Trihydroxide

All present enzymatic activity of Crystal Structure of Human Glutathione S-Transferase M1A-1A Complexed with Glutathionyl-Zinc-Trihydroxide:
2.5.1.18;

Protein crystallography data

The structure of Crystal Structure of Human Glutathione S-Transferase M1A-1A Complexed with Glutathionyl-Zinc-Trihydroxide, PDB code: 1yj6 was solved by Y.V.Patskovsky, L.N.Patskovska, I.Listowsky, S.C.Almo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 2.50
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 178.640, 51.410, 93.820, 90.00, 122.47, 90.00
R / Rfree (%) 23 / 26.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Human Glutathione S-Transferase M1A-1A Complexed with Glutathionyl-Zinc-Trihydroxide (pdb code 1yj6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 3 binding sites of Zinc where determined in the Crystal Structure of Human Glutathione S-Transferase M1A-1A Complexed with Glutathionyl-Zinc-Trihydroxide, PDB code: 1yj6:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 1yj6

Go back to Zinc Binding Sites List in 1yj6
Zinc binding site 1 out of 3 in the Crystal Structure of Human Glutathione S-Transferase M1A-1A Complexed with Glutathionyl-Zinc-Trihydroxide


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 Human Glutathione S-Transferase M1A-1A Complexed with Glutathionyl-Zinc-Trihydroxide within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn219

b:26.8
occ:1.00
O A:HOH259 1.9 41.2 1.0
O A:HOH257 1.9 26.9 1.0
O A:HOH258 1.9 20.4 1.0
SG2 A:GSH218 2.2 40.2 1.0
CB2 A:GSH218 3.4 33.8 1.0
CA2 A:GSH218 4.4 36.2 1.0
OH A:TYR6 4.4 22.4 1.0
OH A:TYR115 4.4 40.6 1.0
CE2 A:TYR115 4.9 44.9 1.0
CZ A:TYR115 4.9 47.2 1.0
N2 A:GSH218 5.0 34.0 1.0

Zinc binding site 2 out of 3 in 1yj6

Go back to Zinc Binding Sites List in 1yj6
Zinc binding site 2 out of 3 in the Crystal Structure of Human Glutathione S-Transferase M1A-1A Complexed with Glutathionyl-Zinc-Trihydroxide


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 Human Glutathione S-Transferase M1A-1A Complexed with Glutathionyl-Zinc-Trihydroxide within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn219

b:42.8
occ:1.00
O B:HOH253 1.8 50.7 1.0
O B:HOH252 1.9 31.3 1.0
SG2 B:GSH218 2.0 65.2 1.0
O B:HOH251 2.0 40.4 1.0
CB2 B:GSH218 3.0 47.5 1.0
CA2 B:GSH218 4.1 47.6 1.0
OH B:TYR6 4.4 35.1 1.0
O B:HOH238 4.7 51.6 1.0
OH B:TYR115 4.7 72.2 1.0
N2 B:GSH218 4.7 44.0 1.0
CD1 B:LEU12 4.8 25.7 1.0
CG B:LEU12 4.8 35.8 1.0

Zinc binding site 3 out of 3 in 1yj6

Go back to Zinc Binding Sites List in 1yj6
Zinc binding site 3 out of 3 in the Crystal Structure of Human Glutathione S-Transferase M1A-1A Complexed with Glutathionyl-Zinc-Trihydroxide


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Crystal Structure of Human Glutathione S-Transferase M1A-1A Complexed with Glutathionyl-Zinc-Trihydroxide within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn219

b:34.2
occ:1.00
O C:HOH249 1.9 42.8 1.0
O C:HOH251 1.9 40.3 1.0
O C:HOH250 1.9 49.8 1.0
SG2 C:GSH218 2.0 52.5 1.0
CB2 C:GSH218 2.9 49.9 1.0
CA2 C:GSH218 3.7 50.3 1.0
N2 C:GSH218 4.4 47.8 1.0
OH C:TYR6 4.5 45.5 1.0
OH C:TYR115 4.6 77.2 1.0
CD1 C:LEU12 4.8 27.8 1.0
C2 C:GSH218 4.8 50.8 1.0
O2 C:GSH218 4.8 51.9 1.0
OE1 C:GSH218 4.9 46.5 1.0
CD1 C:GSH218 4.9 46.1 1.0

Reference:

Y.V.Patskovsky, L.N.Patskovska, I.Listowsky, S.C.Almo. Human Glutathione S-Transferase M1A-1A Catalyzes Formation of Gsh-Metal Complexes To Be Published.
Page generated: Wed Oct 16 20:58:12 2024

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