Zinc in PDB 4bt4: Acetolactate Decarboxylase with A Bound (2S,3S)-2,3- Dihydroxy-2-Methylbutanoic Acid

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

The structure of Acetolactate Decarboxylase with A Bound (2S,3S)-2,3- Dihydroxy-2-Methylbutanoic Acid, PDB code: 4bt4 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)	40.70 / 1.60
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	46.830, 46.830, 198.280, 90.00, 90.00, 120.00
R / Rfree (%)	17.972 / 21.028

The binding sites of Zinc atom in the Acetolactate Decarboxylase with A Bound (2S,3S)-2,3- Dihydroxy-2-Methylbutanoic Acid (pdb code 4bt4). 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 (2S,3S)-2,3- Dihydroxy-2-Methylbutanoic Acid, PDB code: 4bt4:

Zinc binding site 1 out of 1 in the Acetolactate Decarboxylase with A Bound (2S,3S)-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 (2S,3S)-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 2.0 6.7 1.0 OA2 A:QFH302 2.0 2.0 1.0 ND1 A:HIS207 2.1 7.0 1.0 OA3 A:QFH302 2.1 6.8 1.0 NE2 A:HIS196 2.1 6.7 1.0 CA1 A:QFH302 2.9 2.0 1.0 CE1 A:HIS207 2.9 7.2 1.0 CE1 A:HIS194 3.0 6.7 1.0 CA2 A:QFH302 3.0 2.0 1.0 CE1 A:HIS196 3.1 6.7 1.0 CD2 A:HIS194 3.1 6.7 1.0 CD2 A:HIS196 3.1 6.6 1.0 CG A:HIS207 3.2 7.2 1.0 CB A:HIS207 3.7 7.1 1.0 OE1 A:GLU65 3.8 6.6 1.0 CA3 A:QFH302 3.9 2.0 1.0 NE2 A:HIS207 4.1 7.3 1.0 OA1 A:QFH302 4.1 2.0 1.0 ND1 A:HIS194 4.1 6.7 1.0 OA4 A:QFH302 4.2 4.7 1.0 NH2 A:ARG145 4.2 7.6 1.0 CG A:HIS194 4.2 6.7 1.0 ND1 A:HIS196 4.2 6.7 1.0 C3 A:QFH302 4.2 2.0 1.0 CG A:HIS196 4.3 6.6 1.0 CD2 A:HIS207 4.3 7.3 1.0 CA A:HIS207 4.6 7.0 1.0 CD A:GLU65 4.8 6.8 1.0

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