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Zinc in PDB 7et9: Crystal Structure of Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii

Enzymatic activity of Crystal Structure of Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii

All present enzymatic activity of Crystal Structure of Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii:
4.1.2.52;

Protein crystallography data

The structure of Crystal Structure of Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii, PDB code: 7et9 was solved by P.Watthaisong, A.Binlaeh, A.Jaruwat, P.Chaiyen, P.Chitnumsub, S.Maenpuen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.88 / 1.90
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 147.919, 89.669, 86.491, 90, 122.74, 90
R / Rfree (%) 15.5 / 18.5

Other elements in 7et9:

The structure of Crystal Structure of Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii (pdb code 7et9). 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 Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii, PDB code: 7et9:
Jump to Zinc binding site number: 1; 2; 3;

Zinc binding site 1 out of 3 in 7et9

Go back to Zinc Binding Sites List in 7et9
Zinc binding site 1 out of 3 in the Crystal Structure of Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii


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 Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn302

b:12.2
occ:1.00
 O3 A:PYR301 2.0 13.4 1.0
OE2 A:GLU151 2.0 9.4 1.0
OD2 A:ASP177 2.1 8.9 1.0
O A:HOH434 2.1 4.8 1.0
O2 A:PYR301 2.3 12.2 1.0
C2 A:PYR301 2.8 15.6 1.0
CD A:GLU151 3.0 9.9 1.0
C1 A:PYR301 3.0 16.4 1.0
CG A:ASP177 3.1 8.8 1.0
OE1 A:GLU151 3.3 9.3 1.0
CB A:ASP177 3.5 8.8 1.0
NE2 A:GLN149 3.6 9.7 1.0
O A:HOH418 3.8 9.5 1.0
NH1 A:ARG72 3.9 8.9 1.0
C3 A:PYR301 4.1 16.8 1.0
OD1 A:ASP177 4.2 8.7 1.0
O1 A:PYR301 4.3 14.6 1.0
CG A:GLU151 4.3 9.4 1.0
N A:ASP177 4.4 9.1 1.0
O B:VAL120 4.4 8.3 1.0
CA A:GLY174 4.5 11.3 1.0
CD A:GLN149 4.5 9.2 1.0
OE1 A:GLU46 4.5 9.7 1.0
CA A:ASP177 4.6 8.9 1.0
CB A:GLU151 4.6 9.3 1.0
OE1 A:GLN149 4.7 9.7 1.0
CZ A:ARG72 4.9 8.4 1.0

Zinc binding site 2 out of 3 in 7et9

Go back to Zinc Binding Sites List in 7et9
Zinc binding site 2 out of 3 in the Crystal Structure of Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii


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 Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn301

b:12.9
occ:1.00
 O3 B:PYR300 2.0 14.3 1.0
OE2 B:GLU151 2.0 10.1 1.0
OD2 B:ASP177 2.1 9.0 1.0
O B:HOH424 2.2 6.8 1.0
O1 B:PYR300 2.3 11.7 1.0
C2 B:PYR300 2.8 15.8 1.0
C1 B:PYR300 3.0 16.2 1.0
CD B:GLU151 3.0 10.1 1.0
CG B:ASP177 3.1 8.5 1.0
OE1 B:GLU151 3.4 9.5 1.0
CB B:ASP177 3.5 8.7 1.0
NE2 B:GLN149 3.6 10.0 1.0
O B:HOH427 3.8 9.4 1.0
NH1 B:ARG72 4.0 9.0 1.0
C3 B:PYR300 4.1 17.1 1.0
OD1 B:ASP177 4.2 8.0 1.0
O2 B:PYR300 4.3 13.9 1.0
CG B:GLU151 4.3 9.7 1.0
N B:ASP177 4.4 8.9 1.0
O C:VAL120 4.5 7.9 1.0
CA B:GLY174 4.5 11.3 1.0
OE1 B:GLU46 4.5 9.4 1.0
CD B:GLN149 4.5 9.6 1.0
CA B:ASP177 4.5 8.9 1.0
CB B:GLU151 4.6 9.5 1.0
OE1 B:GLN149 4.7 10.6 1.0
CZ B:ARG72 5.0 8.4 1.0
C B:GLY174 5.0 11.2 1.0

Zinc binding site 3 out of 3 in 7et9

Go back to Zinc Binding Sites List in 7et9
Zinc binding site 3 out of 3 in the Crystal Structure of Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii


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 Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Zn301

b:12.4
occ:1.00
 O3 C:PYR300 2.0 15.1 1.0
OE2 C:GLU151 2.0 9.6 1.0
O C:HOH435 2.1 7.3 1.0
OD2 C:ASP177 2.1 9.8 1.0
O1 C:PYR300 2.3 12.5 1.0
C2 C:PYR300 2.8 16.2 1.0
CD C:GLU151 3.0 9.8 1.0
C1 C:PYR300 3.0 16.5 1.0
CG C:ASP177 3.1 9.5 1.0
OE1 C:GLU151 3.4 9.2 1.0
CB C:ASP177 3.5 9.3 1.0
NE2 C:GLN149 3.6 9.9 1.0
O C:HOH426 3.8 8.8 1.0
NH1 C:ARG72 4.0 9.0 1.0
C3 C:PYR300 4.1 17.6 1.0
OD1 C:ASP177 4.3 9.2 1.0
O2 C:PYR300 4.3 14.2 1.0
CG C:GLU151 4.3 9.3 1.0
N C:ASP177 4.4 9.6 1.0
O A:VAL120 4.4 8.2 1.0
CA C:GLY174 4.5 11.3 1.0
OE1 C:GLU46 4.5 8.5 1.0
CD C:GLN149 4.5 9.5 1.0
CA C:ASP177 4.6 9.4 1.0
CB C:GLU151 4.6 9.3 1.0
OE1 C:GLN149 4.7 10.5 1.0
CZ C:ARG72 5.0 8.3 1.0

Reference:

P.Watthaisong, A.Binlaeh, A.Jaruwat, N.Lawan, J.Tantipisit, J.Jaroensuk, L.Chuaboon, J.Phonbuppha, R.Tinikul, P.Chaiyen, P.Chitnumsub, S.Maenpuen. Catalytic and Structural Insights Into A Stereospecific and Thermostable Class II Aldolase Hpai From Acinetobacter Baumannii. J.Biol.Chem. 01280 2021.
ISSN: ESSN 1083-351X
PubMed: 34624314
DOI: 10.1016/J.JBC.2021.101280
Page generated: Tue Oct 29 20:00:07 2024

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