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Zinc in PDB 4opn: Crystal Structure of Mouse Glyoxalase I Complexed with Mah

Enzymatic activity of Crystal Structure of Mouse Glyoxalase I Complexed with Mah

All present enzymatic activity of Crystal Structure of Mouse Glyoxalase I Complexed with Mah:
4.4.1.5;

Protein crystallography data

The structure of Crystal Structure of Mouse Glyoxalase I Complexed with Mah, PDB code: 4opn was solved by J.Zhai, L.Zhang, M.Yuan, H.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 25.61 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 41.559, 65.084, 64.885, 90.00, 101.29, 90.00
R / Rfree (%) 17.7 / 23.1

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Mouse Glyoxalase I Complexed with Mah (pdb code 4opn). 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 Mouse Glyoxalase I Complexed with Mah, PDB code: 4opn:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 4opn

Go back to Zinc Binding Sites List in 4opn
Zinc binding site 1 out of 2 in the Crystal Structure of Mouse Glyoxalase I Complexed with Mah


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 Mouse Glyoxalase I Complexed with Mah within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn201

b:19.8
occ:1.00
OE1 A:GLU100 2.0 18.9 1.0
NE2 A:GLN34 2.0 15.8 1.0
NE2 B:HIS127 2.2 14.7 1.0
O B:ZBF202 2.2 20.6 1.0
O7 B:ZBF202 2.3 16.4 1.0
CD A:GLU100 2.8 16.4 1.0
N B:ZBF202 3.0 18.4 1.0
C B:ZBF202 3.0 17.4 1.0
OE2 A:GLU100 3.0 20.0 1.0
CE1 B:HIS127 3.0 16.9 1.0
CD A:GLN34 3.1 13.3 1.0
CD2 B:HIS127 3.2 13.7 1.0
OE2 B:GLU173 3.2 16.2 1.0
OE1 A:GLN34 3.4 17.9 1.0
CD B:GLU173 3.8 20.0 1.0
OE1 B:GLU173 3.9 18.3 1.0
O B:HOH338 4.1 11.9 1.0
ND1 B:HIS127 4.2 15.6 1.0
CB A:MET36 4.2 14.9 1.0
C12 B:ZBF202 4.2 15.2 1.0
CG A:GLU100 4.3 18.7 1.0
CG A:MET36 4.3 12.1 1.0
CG B:HIS127 4.3 14.9 1.0
CG A:GLN34 4.4 14.5 1.0
C1 B:ZBF202 4.4 17.4 1.0
CB A:GLU100 4.7 14.5 1.0
C2 B:ZBF202 4.8 13.9 1.0
CZ A:PHE72 4.9 19.3 1.0
C13 B:ZBF202 4.9 21.0 1.0
CG B:GLU173 5.0 14.0 1.0

Zinc binding site 2 out of 2 in 4opn

Go back to Zinc Binding Sites List in 4opn
Zinc binding site 2 out of 2 in the Crystal Structure of Mouse Glyoxalase I Complexed with Mah


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 Mouse Glyoxalase I Complexed with Mah within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn201

b:27.6
occ:1.00
OE1 B:GLU100 2.0 21.9 1.0
NE2 B:GLN34 2.1 17.5 1.0
NE2 A:HIS127 2.2 18.5 1.0
O7 A:ZBF202 2.3 27.6 1.0
O A:ZBF202 2.3 25.2 1.0
CD B:GLU100 2.9 24.3 1.0
N A:ZBF202 3.0 25.0 1.0
C A:ZBF202 3.0 25.5 1.0
CD B:GLN34 3.1 19.7 1.0
CE1 A:HIS127 3.2 18.0 1.0
OE2 A:GLU173 3.2 26.0 1.0
OE2 B:GLU100 3.2 26.8 1.0
CD2 A:HIS127 3.2 19.9 1.0
OE1 B:GLN34 3.5 23.5 1.0
CD A:GLU173 3.7 26.0 1.0
OE1 A:GLU173 3.9 24.4 1.0
O B:HOH347 4.1 21.0 1.0
CB B:MET36 4.2 19.8 1.0
CG B:MET36 4.3 16.5 1.0
C12 A:ZBF202 4.3 30.3 1.0
CG B:GLU100 4.3 21.7 1.0
ND1 A:HIS127 4.3 18.9 1.0
CG A:HIS127 4.4 19.3 1.0
CG B:GLN34 4.4 17.6 1.0
C1 A:ZBF202 4.4 24.3 1.0
CB B:GLU100 4.6 23.0 1.0
CZ B:PHE72 4.8 26.1 1.0
C2 A:ZBF202 4.9 23.1 1.0
CG A:GLU173 4.9 25.9 1.0
CB A:GLU173 4.9 22.5 1.0
C13 A:ZBF202 5.0 31.4 1.0

Reference:

Q.Shi, J.Zhai, Z.Zheng, X.Hu. Reversible Inhibition of Glyoxalase I: Synthesis and Activity Evaluation To Be Published.
Page generated: Wed Dec 16 05:39:23 2020

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