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 / R_free (%)*	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

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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: Sun Jul 6 23:04:16 2025

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