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Iron in PDB 3owo: Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor

Enzymatic activity of Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor

All present enzymatic activity of Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor:
1.1.1.1;

Protein crystallography data

The structure of Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor, PDB code: 3owo was solved by J.H.Moon, H.J.Lee, J.M.Song, S.Y.Park, M.Y.Park, H.M.Park, J.Sun, J.H.Park, J.S.Kim, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.07
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 60.917, 87.510, 124.708, 90.00, 94.70, 90.00
R / Rfree (%) 20.2 / 25.3

Iron Binding Sites:

The binding sites of Iron atom in the Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor (pdb code 3owo). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor, PDB code: 3owo:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 3owo

Go back to Iron Binding Sites List in 3owo
Iron binding site 1 out of 4 in the Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe384

b:23.4
occ:1.00
 OD1 A:ASP194 2.2 20.0 1.0
NE2 A:HIS263 2.2 20.6 1.0
NE2 A:HIS198 2.2 17.4 1.0
NE2 A:HIS277 2.3 41.7 1.0
CG A:ASP194 2.9 21.1 1.0
CD2 A:HIS263 3.0 17.4 1.0
OD2 A:ASP194 3.0 22.9 1.0
CD2 A:HIS198 3.2 16.8 1.0
CE1 A:HIS198 3.2 18.3 1.0
CD2 A:HIS277 3.2 42.1 1.0
CE1 A:HIS277 3.3 42.9 1.0
CE1 A:HIS263 3.3 17.4 1.0
OD1 A:ASN281 3.6 32.8 1.0
CG A:HIS263 4.2 19.3 1.0
ND1 A:HIS198 4.3 17.0 1.0
CG A:HIS198 4.3 16.9 1.0
ND1 A:HIS263 4.4 16.5 1.0
ND1 A:HIS277 4.4 44.0 1.0
CG A:HIS277 4.4 42.7 1.0
CB A:ASP194 4.4 18.6 1.0
O A:ASP194 4.5 16.1 1.0
CG A:ASN281 4.6 26.9 1.0
CA A:ASP194 4.9 16.0 1.0
C A:ASP194 5.0 15.5 1.0

Iron binding site 2 out of 4 in 3owo

Go back to Iron Binding Sites List in 3owo
Iron binding site 2 out of 4 in the Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe384

b:0.1
occ:1.00
 OD1 B:ASP194 2.1 15.0 1.0
NE2 B:HIS263 2.1 24.6 1.0
NE2 B:HIS198 2.2 17.1 1.0
O B:HOH522 2.3 38.9 1.0
O B:HOH507 2.3 29.6 1.0
NE2 B:HIS277 2.3 38.5 1.0
CG B:ASP194 2.9 16.8 1.0
CD2 B:HIS263 3.0 25.1 1.0
OD2 B:ASP194 3.1 17.4 1.0
CE1 B:HIS198 3.1 17.2 1.0
CE1 B:HIS263 3.1 24.4 1.0
CD2 B:HIS198 3.2 15.5 1.0
CE1 B:HIS277 3.3 40.9 1.0
CD2 B:HIS277 3.3 38.8 1.0
OD1 B:ASN281 4.1 36.9 1.0
CG B:HIS263 4.2 25.4 1.0
ND1 B:HIS263 4.2 24.8 1.0
ND1 B:HIS198 4.2 17.1 1.0
CG B:HIS198 4.3 15.9 1.0
CB B:ASP194 4.3 14.7 1.0
ND1 B:HIS277 4.4 38.6 1.0
O B:ASP194 4.4 15.9 1.0
CG B:HIS277 4.5 38.5 1.0
CG B:ASN281 4.5 31.6 1.0
O B:HOH501 4.6 29.1 1.0
ND2 B:ASN281 4.7 34.7 1.0
CA B:ASP194 4.8 15.6 1.0
C B:ASP194 4.9 14.6 1.0

Iron binding site 3 out of 4 in 3owo

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Iron binding site 3 out of 4 in the Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe384

b:33.2
occ:1.00
 OD1 C:ASP194 2.2 32.6 1.0
NE2 C:HIS263 2.2 35.1 1.0
NE2 C:HIS198 2.2 27.2 1.0
NE2 C:HIS277 2.3 66.2 1.0
CG C:ASP194 2.9 33.0 1.0
OD2 C:ASP194 2.9 36.2 1.0
CD2 C:HIS277 3.1 65.8 1.0
CD2 C:HIS263 3.1 34.1 1.0
CD2 C:HIS198 3.2 25.2 1.0
CE1 C:HIS198 3.2 27.7 1.0
CE1 C:HIS263 3.3 34.5 1.0
CE1 C:HIS277 3.3 66.8 1.0
OD1 C:ASN281 3.6 51.4 1.0
CG C:HIS277 4.2 66.4 1.0
CG C:HIS263 4.3 35.6 1.0
CG C:HIS198 4.3 26.0 1.0
ND1 C:HIS198 4.3 26.4 1.0
ND1 C:HIS277 4.3 66.5 1.0
ND1 C:HIS263 4.4 34.5 1.0
CB C:ASP194 4.4 34.2 1.0
O C:ASP194 4.4 30.4 1.0
CG C:ASN281 4.8 49.3 1.0
C C:ASP194 4.9 29.8 1.0
CA C:ASP194 4.9 30.5 1.0

Iron binding site 4 out of 4 in 3owo

Go back to Iron Binding Sites List in 3owo
Iron binding site 4 out of 4 in the Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe384

b:23.9
occ:1.00
 NE2 D:HIS198 2.2 12.5 1.0
NE2 D:HIS263 2.2 18.2 1.0
OD1 D:ASP194 2.2 16.1 1.0
NE2 D:HIS277 2.3 45.0 1.0
O D:HOH510 2.8 27.2 1.0
OD2 D:ASP194 2.9 15.8 1.0
CG D:ASP194 2.9 16.3 1.0
CD2 D:HIS277 3.0 44.6 1.0
CD2 D:HIS263 3.0 16.6 1.0
CE1 D:HIS198 3.1 10.9 1.0
CD2 D:HIS198 3.1 10.2 1.0
CE1 D:HIS263 3.3 17.9 1.0
CE1 D:HIS277 3.3 46.5 1.0
OD1 D:ASN281 4.0 28.9 1.0
ND1 D:HIS198 4.1 13.0 1.0
CG D:HIS198 4.2 12.1 1.0
CG D:HIS277 4.2 43.2 1.0
CG D:HIS263 4.3 17.8 1.0
ND1 D:HIS277 4.4 45.0 1.0
ND1 D:HIS263 4.4 17.6 1.0
CB D:ASP194 4.4 13.3 1.0
O D:ASP194 4.5 15.0 1.0
CG D:ASN281 4.7 25.0 1.0
CA D:ASP194 4.9 13.5 1.0
C D:ASP194 4.9 13.7 1.0

Reference:

J.H.Moon, H.J.Lee, S.Y.Park, J.M.Song, M.Y.Park, H.M.Park, J.Sun, J.H.Park, B.Y.Kim, J.S.Kim. Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 with and Without Nad+ Cofactor J.Mol.Biol. V. 407 413 2011.
ISSN: ISSN 0022-2836
PubMed: 21295587
DOI: 10.1016/J.JMB.2011.01.045
Page generated: Sun Aug 4 17:18:56 2024

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