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Iron in PDB 3ox4: Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 Complexed with Nad Cofactor

Enzymatic activity of Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 Complexed with Nad Cofactor

All present enzymatic activity of Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 Complexed with Nad Cofactor:
1.1.1.1;

Protein crystallography data

The structure of Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 Complexed with Nad Cofactor, PDB code: 3ox4 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) 28.75 / 2.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 60.514, 86.965, 124.475, 90.00, 94.83, 90.00
R / Rfree (%) 21.2 / 25.2

Iron Binding Sites:

The binding sites of Iron atom in the Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 Complexed with Nad Cofactor (pdb code 3ox4). 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 Complexed with Nad Cofactor, PDB code: 3ox4:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 3ox4

Go back to Iron Binding Sites List in 3ox4
Iron binding site 1 out of 4 in the Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 Complexed with 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 Complexed with Nad Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:24.4
occ:1.00
 NE2 A:HIS263 2.1 15.4 1.0
OD1 A:ASP194 2.1 23.3 1.0
NE2 A:HIS198 2.2 22.2 1.0
NE2 A:HIS277 2.5 72.1 1.0
CG A:ASP194 2.8 23.1 1.0
OD2 A:ASP194 2.8 24.0 1.0
CD2 A:HIS263 3.0 14.0 1.0
CD2 A:HIS198 3.1 20.6 1.0
CE1 A:HIS263 3.1 16.9 1.0
C5N A:NAD1385 3.1 52.9 1.0
CE1 A:HIS198 3.2 20.9 1.0
CD2 A:HIS277 3.3 71.8 1.0
CE1 A:HIS277 3.5 72.2 1.0
C4N A:NAD1385 3.7 52.8 1.0
OD1 A:ASN281 4.1 32.7 1.0
C6N A:NAD1385 4.1 53.2 1.0
CG A:HIS263 4.2 17.3 1.0
ND1 A:HIS263 4.2 17.3 1.0
CG A:HIS198 4.2 20.5 1.0
ND1 A:HIS198 4.2 20.0 1.0
CB A:ASP194 4.3 20.2 1.0
O A:ASP194 4.5 16.9 1.0
CG A:ASN281 4.5 30.1 1.0
CG A:HIS277 4.5 71.6 1.0
ND1 A:HIS277 4.6 72.0 1.0
ND2 A:ASN281 4.7 29.2 1.0
CA A:ASP194 4.8 17.5 1.0
C A:ASP194 4.9 16.0 1.0
CD1 A:LEU259 4.9 14.3 1.0
C3N A:NAD1385 5.0 54.6 1.0

Iron binding site 2 out of 4 in 3ox4

Go back to Iron Binding Sites List in 3ox4
Iron binding site 2 out of 4 in the Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 Complexed with 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 Complexed with Nad Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:14.1
occ:1.00
 OD1 B:ASP194 2.1 11.8 1.0
NE2 B:HIS263 2.1 17.4 1.0
NE2 B:HIS198 2.2 13.6 1.0
NE2 B:HIS277 2.2 37.4 1.0
CG B:ASP194 2.8 13.6 1.0
CD2 B:HIS263 3.0 14.5 1.0
OD2 B:ASP194 3.0 17.2 1.0
CD2 B:HIS198 3.1 13.5 1.0
CE1 B:HIS198 3.1 12.9 1.0
CE1 B:HIS263 3.2 15.4 1.0
CE1 B:HIS277 3.2 39.9 1.0
CD2 B:HIS277 3.2 39.0 1.0
C5N B:NAD1385 3.5 50.7 1.0
OD1 B:ASN281 4.0 25.9 1.0
C6N B:NAD1385 4.1 49.6 1.0
CG B:HIS263 4.2 15.4 1.0
ND1 B:HIS198 4.2 13.8 1.0
CG B:HIS198 4.2 13.7 1.0
ND1 B:HIS263 4.2 15.0 1.0
CB B:ASP194 4.3 12.0 1.0
ND1 B:HIS277 4.3 40.1 1.0
O B:ASP194 4.3 12.3 1.0
CG B:HIS277 4.4 40.5 1.0
CG B:ASN281 4.5 22.6 1.0
C4N B:NAD1385 4.6 50.5 1.0
CA B:ASP194 4.8 13.3 1.0
C B:ASP194 4.8 14.7 1.0
ND2 B:ASN281 5.0 24.4 1.0

Iron binding site 3 out of 4 in 3ox4

Go back to Iron Binding Sites List in 3ox4
Iron binding site 3 out of 4 in the Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 Complexed with 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 Complexed with Nad Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:26.0
occ:1.00
 OD1 C:ASP194 2.1 27.7 1.0
NE2 C:HIS263 2.1 33.4 1.0
NE2 C:HIS198 2.3 26.8 1.0
CG C:ASP194 2.8 28.9 1.0
OD2 C:ASP194 2.8 31.4 1.0
CE1 C:HIS277 3.0 74.5 1.0
CD2 C:HIS263 3.0 33.2 1.0
CD2 C:HIS198 3.1 26.4 1.0
C5N C:NAD1385 3.2 52.1 1.0
CE1 C:HIS263 3.2 32.5 1.0
NE2 C:HIS277 3.3 75.6 1.0
CE1 C:HIS198 3.3 28.4 1.0
C4N C:NAD1385 3.4 52.4 1.0
OD1 C:ASN281 3.4 47.5 1.0
ND1 C:HIS277 3.7 73.9 1.0
CD2 C:HIS277 4.2 74.5 1.0
CG C:HIS263 4.2 33.5 1.0
C6N C:NAD1385 4.2 52.0 1.0
CB C:ASP194 4.3 28.1 1.0
ND1 C:HIS263 4.3 33.3 1.0
CG C:HIS198 4.3 27.8 1.0
ND1 C:HIS198 4.3 28.0 1.0
O C:ASP194 4.4 31.4 1.0
CG C:HIS277 4.4 73.8 1.0
CG C:ASN281 4.5 45.9 1.0
C3N C:NAD1385 4.6 53.5 1.0
CA C:ASP194 4.9 32.4 1.0
C C:ASP194 4.9 33.1 1.0

Iron binding site 4 out of 4 in 3ox4

Go back to Iron Binding Sites List in 3ox4
Iron binding site 4 out of 4 in the Structures of Iron-Dependent Alcohol Dehydrogenase 2 From Zymomonas Mobilis ZM4 Complexed with 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 Complexed with Nad Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:20.6
occ:1.00
 OD1 D:ASP194 2.1 17.4 1.0
NE2 D:HIS263 2.1 17.7 1.0
NE2 D:HIS198 2.2 17.4 1.0
NE2 D:HIS277 2.3 45.8 1.0
CG D:ASP194 2.9 15.4 1.0
OD2 D:ASP194 2.9 17.8 1.0
CD2 D:HIS263 3.0 17.4 1.0
CE1 D:HIS198 3.0 16.3 1.0
CD2 D:HIS198 3.1 15.0 1.0
C5N D:NAD1385 3.1 53.2 1.0
CD2 D:HIS277 3.2 45.3 1.0
CE1 D:HIS263 3.2 20.6 1.0
CE1 D:HIS277 3.3 47.2 1.0
C4N D:NAD1385 3.4 53.2 1.0
OD1 D:ASN281 4.0 38.3 1.0
C6N D:NAD1385 4.0 52.2 1.0
ND1 D:HIS198 4.1 19.1 1.0
CG D:HIS198 4.2 14.8 1.0
CG D:HIS263 4.2 19.2 1.0
ND1 D:HIS263 4.3 17.3 1.0
CB D:ASP194 4.3 13.9 1.0
C3N D:NAD1385 4.4 54.4 1.0
CG D:HIS277 4.4 46.1 1.0
O D:ASP194 4.4 15.8 1.0
ND1 D:HIS277 4.4 47.5 1.0
CG D:ASN281 4.5 35.0 1.0
CA D:ASP194 4.8 14.9 1.0
C D:ASP194 4.8 14.7 1.0
N1N D:NAD1385 4.9 52.9 1.0
ND2 D:ASN281 5.0 34.9 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 17:19:03 2024

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