Atomistry » Zinc » PDB 5g2u-5gl7 » 5gk8
Atomistry »
  Zinc »
    PDB 5g2u-5gl7 »
      5gk8 »

Zinc in PDB 5gk8: Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form

Enzymatic activity of Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form

All present enzymatic activity of Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form:
4.1.2.13;

Protein crystallography data

The structure of Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form, PDB code: 5gk8 was solved by T.H.Tran, K.H.Huynh, T.H.Ho, L.W.Kang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 36.61 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 66.598, 73.351, 78.269, 90.00, 102.63, 90.00
R / Rfree (%) 16.1 / 20

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form (pdb code 5gk8). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form, PDB code: 5gk8:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 5gk8

Go back to Zinc Binding Sites List in 5gk8
Zinc binding site 1 out of 4 in the Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn405

b:26.5
occ:0.71
OE1 A:GLU174 2.3 24.8 1.0
CE1 A:HIS110 2.3 23.4 1.0
NE2 A:HIS226 2.3 36.4 1.0
OE2 A:GLU174 2.4 32.2 1.0
ND1 A:HIS264 2.6 32.5 1.0
CD A:GLU174 2.6 24.4 1.0
O A:HOH509 2.7 29.3 1.0
CD2 A:HIS226 3.1 37.8 1.0
NE2 A:HIS110 3.1 24.1 1.0
ND1 A:HIS110 3.3 28.0 1.0
CE1 A:HIS226 3.4 37.2 1.0
CE1 A:HIS264 3.4 31.1 1.0
CG A:HIS264 3.7 26.9 1.0
ZN A:ZN406 3.7 32.8 0.6
CB A:HIS264 4.0 22.6 1.0
O A:HOH540 4.0 35.4 1.0
CG A:GLU174 4.1 21.4 1.0
O A:HOH653 4.1 44.0 1.0
OD2 A:ASP144 4.2 24.4 1.0
CG A:HIS226 4.3 40.5 1.0
CD2 A:HIS110 4.3 22.8 1.0
ND1 A:HIS226 4.4 43.0 1.0
CG A:HIS110 4.4 26.8 1.0
NE2 A:HIS264 4.6 18.2 1.0
CD2 A:HIS264 4.7 24.1 1.0
CG A:ASP144 4.8 25.1 1.0
CB A:GLU174 4.9 18.3 1.0

Zinc binding site 2 out of 4 in 5gk8

Go back to Zinc Binding Sites List in 5gk8
Zinc binding site 2 out of 4 in the Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn406

b:32.8
occ:0.58
NE2 A:HIS110 2.0 24.1 1.0
O A:HOH645 2.4 35.6 1.0
O A:HOH521 2.6 27.0 1.0
O A:HOH655 2.9 45.1 1.0
CD2 A:HIS110 3.0 22.8 1.0
ND1 A:HIS264 3.0 32.5 1.0
CE1 A:HIS110 3.1 23.4 1.0
CG A:HIS264 3.3 26.9 1.0
CB A:HIS264 3.5 22.6 1.0
CD2 A:HIS226 3.6 37.8 1.0
CE1 A:HIS264 3.7 31.1 1.0
ZN A:ZN405 3.7 26.5 0.7
ND2 A:ASN286 4.1 16.8 1.0
CG A:HIS110 4.1 26.8 1.0
ND1 A:HIS110 4.1 28.0 1.0
NE2 A:HIS226 4.2 36.4 1.0
CD2 A:HIS264 4.2 24.1 1.0
OD2 A:ASP109 4.4 24.9 1.0
OD1 A:ASP109 4.4 24.4 1.0
NE2 A:HIS264 4.4 18.2 1.0
CA A:HIS264 4.4 24.6 1.0
CG A:HIS226 4.5 40.5 1.0
N A:GLY265 4.8 31.4 1.0
CG A:ASP109 4.8 22.8 1.0
CG A:ASN286 4.9 21.0 1.0
CB A:ASN286 5.0 18.0 1.0

Zinc binding site 3 out of 4 in 5gk8

Go back to Zinc Binding Sites List in 5gk8
Zinc binding site 3 out of 4 in the Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn404

b:28.6
occ:0.67
CE1 B:HIS110 2.1 23.0 1.0
OE1 B:GLU174 2.2 26.7 1.0
NE2 B:HIS226 2.3 38.2 1.0
OE2 B:GLU174 2.5 31.1 1.0
O B:HOH543 2.5 25.9 1.0
CD B:GLU174 2.7 28.9 1.0
NE2 B:HIS110 2.9 27.4 1.0
ND1 B:HIS264 3.1 36.9 1.0
CD2 B:HIS226 3.2 42.2 1.0
ND1 B:HIS110 3.2 25.6 1.0
CE1 B:HIS226 3.3 40.8 1.0
ZN B:ZN405 3.7 30.8 0.6
CG B:HIS264 3.7 31.5 1.0
CE1 B:HIS264 3.7 34.5 1.0
CB B:HIS264 4.0 26.8 1.0
O B:HOH545 4.1 33.8 1.0
OD2 B:ASP144 4.1 28.2 1.0
CG B:GLU174 4.1 22.9 1.0
CD2 B:HIS110 4.2 19.9 1.0
CE B:MET142 4.2 33.4 1.0
CG B:HIS110 4.3 26.5 1.0
CG B:HIS226 4.3 41.2 1.0
ND1 B:HIS226 4.3 44.2 1.0
NE2 B:HIS264 4.5 24.7 1.0
CD2 B:HIS264 4.5 28.3 1.0
CG B:ASP144 4.7 27.0 1.0
CB B:GLU174 4.8 18.3 1.0

Zinc binding site 4 out of 4 in 5gk8

Go back to Zinc Binding Sites List in 5gk8
Zinc binding site 4 out of 4 in the Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn405

b:30.8
occ:0.60
NE2 B:HIS110 2.0 27.4 1.0
ND1 B:HIS264 2.4 36.9 1.0
O B:HOH658 2.4 38.3 1.0
O B:HOH640 2.5 33.9 1.0
O B:HOH531 2.6 25.7 1.0
CD2 B:HIS110 2.9 19.9 1.0
CE1 B:HIS110 3.1 23.0 1.0
CG B:HIS264 3.2 31.5 1.0
CB B:HIS264 3.4 26.8 1.0
CE1 B:HIS264 3.4 34.5 1.0
CD2 B:HIS226 3.6 42.2 1.0
ZN B:ZN404 3.7 28.6 0.7
NE2 B:HIS226 4.1 38.2 1.0
CG B:HIS110 4.1 26.5 1.0
ND1 B:HIS110 4.2 25.6 1.0
ND2 B:ASN286 4.2 22.4 1.0
CA B:HIS264 4.3 24.6 1.0
CG B:HIS226 4.3 41.2 1.0
CD2 B:HIS264 4.4 28.3 1.0
OD2 B:ASP109 4.4 23.7 1.0
NE2 B:HIS264 4.4 24.7 1.0
OD1 B:ASP109 4.4 21.3 1.0
N B:GLY265 4.6 29.9 1.0
CG B:ASP109 4.9 25.4 1.0
CB B:HIS226 4.9 46.6 1.0
CE1 B:HIS226 4.9 40.8 1.0
C B:HIS264 4.9 28.9 1.0

Reference:

T.H.Tran, K.H.Huynh, T.H.Ho, L.W.Kang. Structure of E.Coli Fructose 1,6-Bisphosphate Aldolase, Acetate Bound Form To Be Published.
Page generated: Sun Oct 27 17:05:34 2024

Last articles

As in 2VDL
As in 2VEQ
As in 2VDK
As in 2V5C
As in 2V96
As in 2RA8
As in 2PQ3
As in 2OUI
As in 2RL7
As in 2O4Q
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy