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Zinc in PDB 1r43: Crystal Structure of Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein)

Enzymatic activity of Crystal Structure of Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein)

All present enzymatic activity of Crystal Structure of Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein):
3.5.1.6;

Protein crystallography data

The structure of Crystal Structure of Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein), PDB code: 1r43 was solved by S.Lundgren, Z.Gojkovic, J.Piskur, D.Dobritzsch, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.75 / 2.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 60.430, 77.630, 110.570, 90.00, 95.63, 90.00
R / Rfree (%) 21.1 / 27.4

Zinc Binding Sites:

The binding sites of Zinc atom in the Crystal Structure of Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein) (pdb code 1r43). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein), PDB code: 1r43:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 1r43

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Zinc binding site 1 out of 4 in the Crystal Structure of Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein)


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 Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn500

b:21.5
occ:1.00
OD2 A:ASP125 2.0 23.2 1.0
NE2 A:HIS114 2.1 22.8 1.0
NE2 A:HIS226 2.1 20.5 1.0
O A:HOH546 2.4 11.0 1.0
O A:HOH559 2.4 18.9 1.0
CE1 A:HIS226 2.7 21.0 1.0
CE1 A:HIS114 3.0 23.2 1.0
ZN A:ZN501 3.0 28.1 1.0
CG A:ASP125 3.1 22.8 1.0
CD2 A:HIS114 3.2 23.1 1.0
OE1 A:GLU159 3.2 31.3 1.0
CD2 A:HIS226 3.3 19.5 1.0
OD1 A:ASP125 3.4 26.4 1.0
OE2 A:GLU160 3.5 23.5 1.0
OE1 A:GLN229 3.9 22.2 1.0
N A:GLY126 4.0 22.5 1.0
ND1 A:HIS226 4.0 20.4 1.0
CD A:GLU159 4.1 28.2 1.0
ND1 A:HIS114 4.1 22.9 1.0
ND1 A:HIS397 4.2 22.6 1.0
CG A:HIS114 4.3 22.9 1.0
CG A:HIS226 4.3 19.0 1.0
CA A:GLY126 4.3 22.1 1.0
CD A:GLU160 4.3 23.8 1.0
OE2 A:GLU159 4.4 28.4 1.0
CB A:ASP125 4.4 22.1 1.0
C A:ASP125 4.4 22.3 1.0
O A:HOH506 4.5 18.2 1.0
OE1 A:GLU160 4.7 24.4 1.0
CA A:ASP125 4.7 22.2 1.0
CE1 A:HIS397 4.8 22.8 1.0

Zinc binding site 2 out of 4 in 1r43

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Zinc binding site 2 out of 4 in the Crystal Structure of Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein)


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 Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn501

b:28.1
occ:1.00
OE2 A:GLU160 2.0 23.5 1.0
OD1 A:ASP125 2.0 26.4 1.0
NE2 A:HIS421 2.1 23.1 1.0
O A:HOH559 2.4 18.9 1.0
OE1 A:GLU160 2.5 24.4 1.0
CD A:GLU160 2.6 23.8 1.0
CE1 A:HIS421 2.9 23.2 1.0
CG A:ASP125 2.9 22.8 1.0
ZN A:ZN500 3.0 21.5 1.0
OD2 A:ASP125 3.1 23.2 1.0
CD2 A:HIS421 3.1 22.3 1.0
OE1 A:GLN229 3.7 22.2 1.0
NE2 A:HIS114 4.0 22.8 1.0
ND1 A:HIS421 4.1 24.1 1.0
CG A:GLU160 4.1 23.1 1.0
CE1 A:HIS114 4.1 23.2 1.0
CG A:HIS421 4.2 23.2 1.0
OE1 A:GLU159 4.2 31.3 1.0
OE2 A:GLU159 4.3 28.4 1.0
CB A:ASP125 4.3 22.1 1.0
OE1 A:GLN118 4.5 22.6 1.0
CD A:GLN229 4.6 20.9 1.0
CE1 A:HIS226 4.6 21.0 1.0
NE2 A:GLN229 4.7 23.5 1.0
CD A:GLU159 4.7 28.2 1.0
NE2 A:HIS226 4.7 20.5 1.0
O A:HOH546 4.8 11.0 1.0
OG A:SER420 4.9 22.1 1.0

Zinc binding site 3 out of 4 in 1r43

Go back to Zinc Binding Sites List in 1r43
Zinc binding site 3 out of 4 in the Crystal Structure of Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein)


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 Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn500

b:20.7
occ:1.00
O B:HOH1519 1.8 18.9 1.0
NE2 B:HIS114 2.1 21.5 1.0
NE2 B:HIS226 2.1 20.9 1.0
OD1 B:ASP125 2.5 19.4 1.0
OE1 B:GLU159 2.7 21.3 1.0
O B:HOH1512 2.8 6.5 1.0
CE1 B:HIS226 2.9 20.4 1.0
CE1 B:HIS114 2.9 21.2 1.0
ZN B:ZN501 2.9 26.9 1.0
CD2 B:HIS114 3.2 21.6 1.0
CD2 B:HIS226 3.2 19.9 1.0
CG B:ASP125 3.5 20.4 1.0
CD B:GLU159 3.7 20.4 1.0
OD2 B:ASP125 3.8 19.6 1.0
N B:GLY126 3.9 21.1 1.0
CA B:GLY126 4.0 21.0 1.0
ND1 B:HIS226 4.1 20.3 1.0
ND1 B:HIS114 4.1 21.7 1.0
O B:HOH1508 4.2 12.2 1.0
CG B:HIS226 4.3 19.9 1.0
CG B:HIS114 4.3 21.6 1.0
OE2 B:GLU159 4.3 18.0 1.0
C B:ASP125 4.4 21.1 1.0
ND1 B:HIS397 4.4 20.4 1.0
OE2 B:GLU160 4.4 22.3 1.0
CE1 B:HIS397 4.6 20.4 1.0
CG B:GLU159 4.7 20.6 1.0
CB B:ASP125 4.8 20.6 1.0
NE2 B:GLN229 4.8 16.9 1.0
OE1 B:GLN229 4.8 17.1 1.0
O B:ASP125 4.9 21.4 1.0
CA B:ASP125 4.9 20.9 1.0
OG B:SER113 4.9 22.3 1.0
CD B:GLU160 5.0 21.1 1.0

Zinc binding site 4 out of 4 in 1r43

Go back to Zinc Binding Sites List in 1r43
Zinc binding site 4 out of 4 in the Crystal Structure of Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein)


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Crystal Structure of Beta-Alanine Synthase From Saccharomyces Kluyveri (Selenomethionine Substituted Protein) within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn501

b:26.9
occ:1.00
OE2 B:GLU160 2.0 22.3 1.0
OD2 B:ASP125 2.3 19.6 1.0
O B:HOH1519 2.5 18.9 1.0
NE2 B:HIS421 2.6 21.3 1.0
CD B:GLU160 2.7 21.1 1.0
OE1 B:GLU160 2.9 20.4 1.0
ZN B:ZN500 2.9 20.7 1.0
OD1 B:ASP125 3.0 19.4 1.0
CG B:ASP125 3.0 20.4 1.0
CE1 B:HIS421 3.5 21.2 1.0
CD2 B:HIS421 3.6 21.3 1.0
OE1 B:GLU159 3.6 21.3 1.0
NE2 B:GLN229 3.8 16.9 1.0
OE2 B:GLU159 3.8 18.0 1.0
CE1 B:HIS114 3.8 21.2 1.0
NE2 B:HIS114 3.9 21.5 1.0
CG B:GLU160 4.0 20.8 1.0
CD B:GLU159 4.1 20.4 1.0
CB B:ASP125 4.5 20.6 1.0
OE1 B:GLN118 4.5 21.9 1.0
NE2 B:HIS226 4.6 20.9 1.0
ND1 B:HIS421 4.6 21.6 1.0
CD B:GLN229 4.7 16.9 1.0
CG B:HIS421 4.7 21.4 1.0
CE1 B:HIS226 4.7 20.4 1.0
OE1 B:GLN229 4.9 17.1 1.0
O B:HOH1512 4.9 6.5 1.0
ND1 B:HIS114 4.9 21.7 1.0

Reference:

S.Lundgren, Z.Gojkovic, J.Piskur, D.Dobritzsch. Yeast Beta-Alanine Synthase Shares A Structural Scaffold and Origin with Dizinc-Dependent Exopeptidases J.Biol.Chem. V. 278 51851.
ISSN: ISSN 0021-9258
PubMed: 14534321
DOI: 10.1074/JBC.M308674200
Page generated: Wed Dec 16 03:02:27 2020

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