Zinc in PDB 4eri: Evidence For A Dual Role of An Active Site Histidine in Alpha-Amino- Beta-Carboxymuconate-Epsilon-Semialdehyde Decarboxylase

The structure of Evidence For A Dual Role of An Active Site Histidine in Alpha-Amino- Beta-Carboxymuconate-Epsilon-Semialdehyde Decarboxylase, PDB code: 4eri was solved by L.Huo, A.J.Fielding, Y.Chen, T.Li, H.Iwaki, J.P.Hosler, L.Chen, Y.Hasegawa, L.Que Jr., A.Liu, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.76 / 2.00
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	153.836, 48.561, 110.201, 90.00, 126.89, 90.00
R / Rfree (%)	20.5 / 25.6

The structure of Evidence For A Dual Role of An Active Site Histidine in Alpha-Amino- Beta-Carboxymuconate-Epsilon-Semialdehyde Decarboxylase also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Zinc atom in the Evidence For A Dual Role of An Active Site Histidine in Alpha-Amino- Beta-Carboxymuconate-Epsilon-Semialdehyde Decarboxylase (pdb code 4eri). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Evidence For A Dual Role of An Active Site Histidine in Alpha-Amino- Beta-Carboxymuconate-Epsilon-Semialdehyde Decarboxylase, PDB code: 4eri:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Evidence For A Dual Role of An Active Site Histidine in Alpha-Amino- Beta-Carboxymuconate-Epsilon-Semialdehyde Decarboxylase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Evidence For A Dual Role of An Active Site Histidine in Alpha-Amino- Beta-Carboxymuconate-Epsilon-Semialdehyde Decarboxylase within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn401 b:28.9 occ:1.00 NE2 A:HIS11 2.2 23.4 1.0 NE2 A:HIS9 2.3 23.9 1.0 NE2 A:HIS177 2.3 24.4 1.0 OD2 A:ASP294 2.4 25.9 1.0 OH A:TYR228 2.4 29.4 1.0 O A:HOH596 2.4 25.4 1.0 CD2 A:HIS11 3.1 22.2 1.0 O A:HOH643 3.1 36.7 1.0 CD2 A:HIS177 3.1 21.1 1.0 CE1 A:HIS11 3.2 21.6 1.0 CE1 A:HIS9 3.2 25.1 1.0 CD2 A:HIS9 3.2 24.7 1.0 CG A:ASP294 3.3 29.6 1.0 CE1 A:HIS177 3.4 27.3 1.0 CZ A:TYR228 3.4 29.1 1.0 OD1 A:ASP294 3.7 31.5 1.0 CE2 A:TYR228 4.0 23.9 1.0 CG A:HIS11 4.3 24.1 1.0 ND1 A:HIS11 4.3 21.7 1.0 ND1 A:HIS9 4.3 25.5 1.0 CG A:HIS177 4.4 24.9 1.0 CE1 A:TYR228 4.4 28.5 1.0 CG A:HIS9 4.4 26.8 1.0 CB A:ASP294 4.4 27.1 1.0 ND1 A:HIS177 4.5 24.6 1.0 CA A:ASP294 4.7 22.4 1.0 O A:HOH647 4.8 37.2 1.0

Zinc binding site 2 out of 2 in the Evidence For A Dual Role of An Active Site Histidine in Alpha-Amino- Beta-Carboxymuconate-Epsilon-Semialdehyde Decarboxylase


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Evidence For A Dual Role of An Active Site Histidine in Alpha-Amino- Beta-Carboxymuconate-Epsilon-Semialdehyde Decarboxylase within 5.0Å range: probe atom residue distance (Å) B Occ B:Zn401 b:41.7 occ:1.00 OD2 B:ASP294 2.3 44.5 1.0 NE2 B:HIS177 2.3 28.5 1.0 NE2 B:HIS9 2.3 36.4 1.0 O B:HOH545 2.4 36.8 1.0 NE2 B:HIS11 2.4 40.4 1.0 OH B:TYR228 2.4 42.0 1.0 CD2 B:HIS11 3.0 42.2 1.0 CG B:ASP294 3.2 44.3 1.0 CE1 B:HIS9 3.2 37.8 1.0 CD2 B:HIS177 3.3 33.2 1.0 CE1 B:HIS177 3.3 39.4 1.0 CD2 B:HIS9 3.3 36.5 1.0 CZ B:TYR228 3.4 40.1 1.0 O B:HOH546 3.4 44.1 1.0 CE1 B:HIS11 3.6 45.2 1.0 OD1 B:ASP294 3.8 46.5 1.0 CE2 B:TYR228 3.9 38.1 1.0 O B:HOH533 4.1 43.0 1.0 CB B:ASP294 4.2 42.8 1.0 CG B:HIS11 4.3 45.8 1.0 CE1 B:TYR228 4.3 40.0 1.0 ND1 B:HIS9 4.3 32.9 1.0 ND1 B:HIS177 4.4 34.5 1.0 CG B:HIS9 4.4 39.8 1.0 CG B:HIS177 4.4 35.6 1.0 CA B:ASP294 4.5 41.6 1.0 ND1 B:HIS11 4.5 42.3 1.0

L.Huo, A.J.Fielding, Y.Chen, T.Li, H.Iwaki, J.P.Hosler, L.Chen, Y.Hasegawa, L.Que, A.Liu. Evidence For A Dual Role of An Active Site Histidine in Alpha-Amino-Beta-Carboxymuconate-Epsilon-Semialdehyde Decarboxylase Biochemistry V. 51 5811 2012.
ISSN: ISSN 0006-2960
PubMed: 22746257
DOI: 10.1021/BI300635B