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Calcium in PDB 3lye: Crystal Structure of Oxaloacetate Acetylhydrolase

Enzymatic activity of Crystal Structure of Oxaloacetate Acetylhydrolase

All present enzymatic activity of Crystal Structure of Oxaloacetate Acetylhydrolase:
3.7.1.1;

Protein crystallography data

The structure of Crystal Structure of Oxaloacetate Acetylhydrolase, PDB code: 3lye was solved by O.Herzberg, C.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.90 / 1.30
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 82.736, 82.736, 73.846, 90.00, 90.00, 90.00
R / Rfree (%) 13.1 / 16.6

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Oxaloacetate Acetylhydrolase (pdb code 3lye). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 3 binding sites of Calcium where determined in the Crystal Structure of Oxaloacetate Acetylhydrolase, PDB code: 3lye:
Jump to Calcium binding site number: 1; 2; 3;

Calcium binding site 1 out of 3 in 3lye

Go back to Calcium Binding Sites List in 3lye
Calcium binding site 1 out of 3 in the Crystal Structure of Oxaloacetate Acetylhydrolase


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 Oxaloacetate Acetylhydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:16.1
occ:1.00
O A:HOH602 2.0 19.5 1.0
O A:HOH601 2.3 17.2 1.0
O A:HOH604 2.4 13.9 1.0
OD1 A:ASP157 2.4 12.5 1.0
O A:HOH603 2.5 19.2 1.0
OD2 A:ASP155 2.5 13.2 1.0
O A:HOH701 2.5 19.4 0.9
CG A:ASP155 3.4 11.0 1.0
CG A:ASP157 3.5 10.0 1.0
OD1 A:ASP155 3.6 10.8 1.0
O A:HOH674 4.0 23.6 0.9
O A:HOH866 4.0 43.5 1.0
OD2 A:ASP157 4.1 12.2 1.0
O A:HOH662 4.3 14.7 0.9
OE2 A:GLU184 4.4 15.6 1.0
OD2 A:ASP126 4.4 16.0 1.0
OD1 A:ASP126 4.4 17.7 1.0
O A:HOH636 4.4 11.6 1.0
CB A:ASP157 4.5 9.8 1.0
O A:HOH665 4.7 24.6 1.0
CA A:GLY114 4.7 9.8 1.0
CA A:ASP157 4.7 9.6 1.0
O A:HOH826 4.7 43.6 1.0
OE1 A:GLU184 4.7 20.4 1.0
CB A:ASP155 4.8 8.7 1.0
CG A:ASP126 4.9 13.9 1.0
NH1 A:ARG229 4.9 18.8 1.0
O A:HOH673 5.0 28.4 1.0
O A:HOH853 5.0 41.9 1.0

Calcium binding site 2 out of 3 in 3lye

Go back to Calcium Binding Sites List in 3lye
Calcium binding site 2 out of 3 in the Crystal Structure of Oxaloacetate Acetylhydrolase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Oxaloacetate Acetylhydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca502

b:13.8
occ:1.00
OE1 A:GLU285 2.3 16.9 1.0
O A:HOH606 2.3 18.5 1.0
OD1 A:ASN286 2.3 13.7 1.0
O A:HOH605 2.4 16.5 1.0
CD A:GLU285 3.4 15.6 1.0
CG A:ASN286 3.4 12.7 1.0
ND2 A:ASN286 3.8 13.0 1.0
OE2 A:GLU285 4.0 16.7 1.0
O A:HOH694 4.3 22.1 1.0
CG A:GLU285 4.4 13.7 1.0
O A:HOH647 4.4 16.0 1.0
O A:HOH653 4.5 21.1 1.0
N A:ASN286 4.7 12.6 1.0
CB A:ASN286 4.7 12.6 1.0
CA A:ASN286 4.8 13.7 1.0

Calcium binding site 3 out of 3 in 3lye

Go back to Calcium Binding Sites List in 3lye
Calcium binding site 3 out of 3 in the Crystal Structure of Oxaloacetate Acetylhydrolase


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 3 of Crystal Structure of Oxaloacetate Acetylhydrolase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca503

b:26.1
occ:1.00
O A:HOH607 2.5 28.9 1.0
O A:HOH608 2.5 28.8 0.9
O A:HOH899 2.5 27.9 0.8
O A:HOH737 2.5 36.9 1.0
O A:PHE148 2.5 19.3 1.0
O A:HOH901 2.6 42.8 0.9
C A:PHE148 3.7 18.4 1.0
NZ A:LYS76 4.1 17.7 1.0
CB A:PHE148 4.2 17.1 1.0
CA A:PHE148 4.5 15.0 1.0
O A:HOH966 4.6 48.3 1.0
O A:HOH733 4.7 19.4 0.8
O A:HOH791 4.7 31.8 0.9
O A:HOH641 4.7 18.5 1.0
N A:GLY149 4.7 15.9 1.0
O A:HOH792 4.7 43.4 1.0
CA A:GLY149 4.8 14.9 1.0

Reference:

C.Chen, Q.Sun, B.Narayanan, D.L.Nuss, O.Herzberg. Structure of Oxalacetate Acetylhydrolase, A Virulence Factor of the Chestnut Blight Fungus. J.Biol.Chem. V. 285 26685 2010.
ISSN: ISSN 0021-9258
PubMed: 20558740
DOI: 10.1074/JBC.M110.117804
Page generated: Sat Dec 12 04:20:01 2020

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