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Zinc in PDB 4bt3: Acetolactate Decarboxylase with A Bound (2R,3R)-2,3- Dihydroxy-2-Methylbutanoic Acid

Enzymatic activity of Acetolactate Decarboxylase with A Bound (2R,3R)-2,3- Dihydroxy-2-Methylbutanoic Acid

All present enzymatic activity of Acetolactate Decarboxylase with A Bound (2R,3R)-2,3- Dihydroxy-2-Methylbutanoic Acid:
4.1.1.5;

Protein crystallography data

The structure of Acetolactate Decarboxylase with A Bound (2R,3R)-2,3- Dihydroxy-2-Methylbutanoic Acid, PDB code: 4bt3 was solved by V.A Marlow, D.Rea, S.Najmudin, M.Wills, V.Fulop, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 34.75 / 1.10
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 47.110, 47.110, 198.910, 90.00, 90.00, 120.00
R / Rfree (%) 20.666 / 22.466

Zinc Binding Sites:

The binding sites of Zinc atom in the Acetolactate Decarboxylase with A Bound (2R,3R)-2,3- Dihydroxy-2-Methylbutanoic Acid (pdb code 4bt3). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Acetolactate Decarboxylase with A Bound (2R,3R)-2,3- Dihydroxy-2-Methylbutanoic Acid, PDB code: 4bt3:

Zinc binding site 1 out of 1 in 4bt3

Go back to Zinc Binding Sites List in 4bt3
Zinc binding site 1 out of 1 in the Acetolactate Decarboxylase with A Bound (2R,3R)-2,3- Dihydroxy-2-Methylbutanoic Acid


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Acetolactate Decarboxylase with A Bound (2R,3R)-2,3- Dihydroxy-2-Methylbutanoic Acid within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn301

b:2.0
occ:1.00
NE2 A:HIS194 2.1 6.0 1.0
NE2 A:HIS196 2.1 5.9 1.0
ND1 A:HIS207 2.1 6.5 1.0
OA3 A:WTZ302 2.2 3.7 1.0
OA1 A:WTZ302 2.2 5.8 1.0
OA4 A:WTZ302 2.4 5.2 1.0
CA2 A:WTZ302 3.0 5.4 1.0
CE1 A:HIS207 3.0 6.7 1.0
CA1 A:WTZ302 3.0 5.0 1.0
CE1 A:HIS194 3.0 6.0 1.0
CD2 A:HIS196 3.1 5.8 1.0
CE1 A:HIS196 3.1 5.9 1.0
CD2 A:HIS194 3.2 6.0 1.0
CG A:HIS207 3.2 6.6 1.0
C3 A:WTZ302 3.3 5.2 1.0
CB A:HIS207 3.7 6.5 1.0
OE1 A:GLU65 3.8 5.9 1.0
NH2 A:ARG145 4.0 7.5 1.0
NE2 A:HIS207 4.2 7.0 1.0
ND1 A:HIS194 4.2 6.0 1.0
OA2 A:WTZ302 4.2 7.9 1.0
ND1 A:HIS196 4.2 5.8 1.0
O A:HOH2384 4.2 7.5 1.0
CG A:HIS196 4.3 5.7 1.0
CG A:HIS194 4.3 6.0 1.0
CD2 A:HIS207 4.3 6.9 1.0
CA3 A:WTZ302 4.4 5.8 1.0
CA5 A:WTZ302 4.6 7.8 1.0
CA A:HIS207 4.6 6.3 1.0
CD A:GLU65 4.8 6.2 1.0
OE1 A:GLU253 4.9 11.6 1.0

Reference:

V.A.Marlow, D.Rea, S.Najmudin, M.Wills, V.Fulop. Structure and Mechanism of Acetolactate Decarboxylase. Acs Chem.Biol. V. 8 2339 2013.
ISSN: ISSN 1554-8929
PubMed: 23985082
DOI: 10.1021/CB400429H
Page generated: Sat Oct 26 19:58:06 2024

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