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Arsenic in PDB 1x1t: Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Pseudomonas Fragi Complexed with Nad+

Enzymatic activity of Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Pseudomonas Fragi Complexed with Nad+

All present enzymatic activity of Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Pseudomonas Fragi Complexed with Nad+:
1.1.1.30;

Protein crystallography data

The structure of Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Pseudomonas Fragi Complexed with Nad+, PDB code: 1x1t was solved by K.Ito, Y.Nakajima, E.Ichihara, K.Ogawa, T.Yoshimoto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 1.52
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 64.765, 99.970, 109.585, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 21.3

Other elements in 1x1t:

The structure of Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Pseudomonas Fragi Complexed with Nad+ also contains other interesting chemical elements:

Magnesium (Mg) 1 atom

Arsenic Binding Sites:

The binding sites of Arsenic atom in the Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Pseudomonas Fragi Complexed with Nad+ (pdb code 1x1t). This binding sites where shown within 5.0 Angstroms radius around Arsenic atom.
In total only one binding site of Arsenic was determined in the Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Pseudomonas Fragi Complexed with Nad+, PDB code: 1x1t:

Arsenic binding site 1 out of 1 in 1x1t

Go back to Arsenic Binding Sites List in 1x1t
Arsenic binding site 1 out of 1 in the Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Pseudomonas Fragi Complexed with Nad+


Mono view


Stereo pair view

A full contact list of Arsenic with other atoms in the As binding site number 1 of Crystal Structure of D-3-Hydroxybutyrate Dehydrogenase From Pseudomonas Fragi Complexed with Nad+ within 5.0Å range:
probe atom residue distance (Å) B Occ
A:As302

b:18.8
occ:1.00
AS A:CAC302 0.0 18.8 1.0
O2 A:CAC302 1.6 18.3 1.0
O1 A:CAC302 1.7 16.3 1.0
C2 A:CAC302 1.8 19.9 1.0
C1 A:CAC302 2.0 15.6 1.0
OH A:TYR155 3.7 11.2 1.0
ND1 A:HIS144 3.7 11.1 1.0
OG A:SER142 3.8 9.8 1.0
CE1 A:TYR155 3.9 9.6 1.0
O A:HOH596 3.9 24.1 1.0
CZ A:TYR155 4.1 9.3 1.0
C5N A:NAD300 4.1 18.4 1.0
C4N A:NAD300 4.2 18.8 1.0
CE1 A:HIS144 4.2 10.4 1.0
CZ3 A:TRP187 4.2 19.3 1.0
NZ A:LYS152 4.3 20.7 1.0
C3N A:NAD300 4.5 18.2 1.0
O7N A:NAD300 4.6 18.0 1.0
CE3 A:TRP187 4.6 17.7 1.0
CH2 A:TRP187 4.7 18.1 1.0
CB A:SER142 4.8 9.3 1.0
C6N A:NAD300 4.8 16.1 1.0
CG A:HIS144 4.9 8.3 1.0
C7N A:NAD300 4.9 18.4 1.0
CD1 A:TYR155 4.9 10.8 1.0
C2N A:NAD300 4.9 17.1 1.0

Reference:

K.Ito, Y.Nakajima, E.Ichihara, K.Ogawa, N.Katayama, K.Nakashima, T.Yoshimoto. D-3-Hydroxybutyrate Dehydrogenase From Pseudomonas Fragi: Molecular Cloning of the Enzyme Gene and Crystal Structure of the Enzyme J.Mol.Biol. V. 355 722 2006.
ISSN: ISSN 0022-2836
PubMed: 16325199
DOI: 10.1016/J.JMB.2005.10.072
Page generated: Wed Jul 10 11:16:22 2024

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