Zinc in PDB 2hbv: Crystal Structure of Alpha-Amino-Beta-Carboxymuconate-Epsilon- Semialdehyde-Decarboxylase (Acmsd)

All present enzymatic activity of Crystal Structure of Alpha-Amino-Beta-Carboxymuconate-Epsilon- Semialdehyde-Decarboxylase (Acmsd):
4.1.1.45;

The structure of Crystal Structure of Alpha-Amino-Beta-Carboxymuconate-Epsilon- Semialdehyde-Decarboxylase (Acmsd), PDB code: 2hbv was solved by D.Martynowski, Y.Eyobo, T.Li, K.Yang, A.Liu, H.Zhang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.81 / 1.65
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	153.557, 48.107, 110.700, 90.00, 127.31, 90.00
R / Rfree (%)	21.1 / 25.1

The structure of Crystal Structure of Alpha-Amino-Beta-Carboxymuconate-Epsilon- Semialdehyde-Decarboxylase (Acmsd) also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Crystal Structure of Alpha-Amino-Beta-Carboxymuconate-Epsilon- Semialdehyde-Decarboxylase (Acmsd) (pdb code 2hbv). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Alpha-Amino-Beta-Carboxymuconate-Epsilon- Semialdehyde-Decarboxylase (Acmsd), PDB code: 2hbv:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Crystal Structure of Alpha-Amino-Beta-Carboxymuconate-Epsilon- Semialdehyde-Decarboxylase (Acmsd)


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 Alpha-Amino-Beta-Carboxymuconate-Epsilon- Semialdehyde-Decarboxylase (Acmsd) within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:44.7 occ:1.00 O A:HOH464 2.0 29.9 1.0 NE2 A:HIS9 2.1 31.2 1.0 OD2 A:ASP294 2.1 30.5 1.0 NE2 A:HIS177 2.2 26.6 1.0 NE2 A:HIS11 2.2 28.2 1.0 O A:HOH501 2.7 50.6 1.0 CE1 A:HIS9 3.0 33.9 1.0 CD2 A:HIS177 3.1 28.3 1.0 CD2 A:HIS11 3.1 28.5 1.0 CD2 A:HIS9 3.1 30.5 1.0 CG A:ASP294 3.1 30.6 1.0 CE1 A:HIS177 3.2 30.4 1.0 CE1 A:HIS11 3.2 27.9 1.0 NE2 A:HIS228 3.3 42.8 1.0 OD1 A:ASP294 3.7 33.2 1.0 CE1 A:HIS228 4.0 39.4 1.0 ND1 A:HIS9 4.2 33.8 1.0 CB A:ASP294 4.2 30.2 1.0 CG A:HIS9 4.3 30.1 1.0 CG A:HIS177 4.3 28.8 1.0 ND1 A:HIS177 4.3 29.0 1.0 CD2 A:HIS228 4.3 39.7 1.0 CG A:HIS11 4.3 27.7 1.0 ND1 A:HIS11 4.3 24.1 1.0 CA A:ASP294 4.6 30.1 1.0 O A:HOH471 4.9 47.2 1.0 O A:HOH593 4.9 43.5 1.0

Zinc binding site 2 out of 2 in the Crystal Structure of Alpha-Amino-Beta-Carboxymuconate-Epsilon- Semialdehyde-Decarboxylase (Acmsd)


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 Alpha-Amino-Beta-Carboxymuconate-Epsilon- Semialdehyde-Decarboxylase (Acmsd) within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn402 b:54.4 occ:1.00 O B:HOH446 2.1 36.4 1.0 OD2 B:ASP294 2.1 44.9 1.0 NE2 B:HIS11 2.2 41.5 1.0 NE2 B:HIS9 2.2 37.7 1.0 O B:HOH432 2.3 44.1 1.0 O B:HOH438 2.3 37.3 1.0 CE1 B:HIS9 3.1 41.1 1.0 CE1 B:HIS11 3.2 41.4 1.0 CD2 B:HIS11 3.2 41.6 1.0 CG B:ASP294 3.2 45.1 1.0 CD2 B:HIS9 3.3 38.4 1.0 OD1 B:ASP294 3.8 45.8 1.0 O B:HOH518 4.1 50.1 1.0 CB B:ASP294 4.2 44.9 1.0 ND1 B:HIS9 4.2 39.8 1.0 ND1 B:HIS177 4.2 42.4 1.0 O B:HOH507 4.3 52.0 1.0 ND1 B:HIS11 4.3 41.5 1.0 CG B:HIS11 4.3 41.7 1.0 CG B:HIS9 4.3 39.1 1.0 CE1 B:HIS177 4.4 44.0 1.0 NE2 B:HIS228 4.5 46.0 1.0 CA B:ASP294 4.5 44.9 1.0

D.Martynowski, Y.Eyobo, T.Li, K.Yang, A.Liu, H.Zhang. Crystal Structure of Alpha-Amino-Beta-Carboxymuconate-Epsilon-Semialdehyde Decarboxylase: Insight Into the Active Site and Catalytic Mechanism of A Novel Decarboxylation Reaction. Biochemistry V. 45 10412 2006.
ISSN: ISSN 0006-2960
PubMed: 16939194
DOI: 10.1021/BI060903Q