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Calcium 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:

Zinc (Zn) 3 atoms

Calcium Binding Sites:

The binding sites of Calcium 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 Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Abhpai-Zn-Pyruvate Complex, Class II Aldolase, Hpai From Acinetobacter Baumannii, PDB code: 7et9:

Calcium binding site 1 out of 1 in 7et9

Go back to Calcium Binding Sites List in 7et9
Calcium binding site 1 out of 1 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 Calcium with other atoms in the Ca 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:Ca303

b:24.4
occ:1.00
 OD2 B:ASP51 2.4 13.0 1.0
OD2 C:ASP51 2.4 11.7 1.0
OD2 A:ASP51 2.4 12.3 1.0
O B:HOH493 2.5 27.1 1.0
O A:HOH467 2.5 29.4 1.0
O C:HOH444 2.7 30.3 1.0
CG B:ASP51 3.4 10.4 1.0
CG C:ASP51 3.5 10.0 1.0
CG A:ASP51 3.5 10.3 1.0
OD1 B:ASP51 4.0 11.0 1.0
OD1 A:ASP51 4.0 10.2 1.0
OD1 C:ASP51 4.0 10.8 1.0
O C:HOH506 4.1 31.0 1.0
O A:HOH503 4.2 30.6 1.0
O B:HOH518 4.2 33.1 1.0
O B:HOH506 4.2 7.3 1.0
O A:HOH539 4.2 26.3 1.0
O A:HOH505 4.3 7.0 1.0
O C:HOH505 4.3 7.1 1.0
CB B:ASP51 4.6 9.3 1.0
CB C:ASP51 4.6 9.1 1.0
CB A:ASP51 4.6 9.2 1.0
CD C:ARG53 4.9 8.7 1.0
CD A:ARG53 4.9 8.5 1.0
CD B:ARG53 4.9 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: Wed Jul 9 21:56:22 2025

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