Chlorine in PDB 5ouj: Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39

Enzymatic activity of Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39

All present enzymatic activity of Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39:
1.1.1.21;

Protein crystallography data

The structure of Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39, PDB code: 5ouj was solved by A.Cousido-Siah, F.X.Ruiz, A.Mitschler, K.Metwally, A.Podjarny, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

*Resolution Low / High (Å)*	28.90 / 0.96
*Space group*	P 1
*Cell size a, b, c (Å), α, β, γ (°)*	40.050, 46.979, 47.283, 76.40, 67.57, 77.40
*R / R_free (%)*	13 / 14.7

Other elements in 5ouj:

The structure of Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39 also contains other interesting chemical elements:

Fluorine

(F)

1 atom

Chlorine Binding Sites:

The binding sites of Chlorine atom in the Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39 (pdb code 5ouj). This binding sites where shown within 5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39, PDB code: 5ouj:

Chlorine binding site 1 out of 1 in 5ouj

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Chlorine Binding Sites List in 5ouj

Chlorine binding site 1 out of 1 in the Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39

Mono view

Stereo pair view

A full contact list of Chlorine with other atoms in the Cl binding site number 1 of Crystal Structure of Human AKR1B1 Complexed with Nadp+ and Compound 39 within 5.0Å range:

probe	atom	residue	distance (Å)	B	Occ
A:Cl402 b:65.7 occ:0.96	CL1	A:AW8402	0.0	65.7	1.0
	C16	A:AW8402	1.8	64.3	1.0
	C14	A:AW8402	2.8	62.8	1.0
	C15	A:AW8402	2.8	62.7	1.0
	O	A:HOH749	3.2	21.8	1.0
	N	A:SER302	3.8	20.9	1.0
	N	A:LEU301	3.9	17.9	1.0
	OG	A:SER302	3.9	25.9	1.0
	C12	A:AW8402	4.1	59.7	1.0
	C13	A:AW8402	4.1	59.6	1.0
	CB	A:SER302	4.2	24.3	1.0
	CB	A:LEU301	4.2	19.5	1.0
	CA	A:LEU301	4.3	19.1	1.0
	C	A:LEU301	4.4	20.0	1.0
	CA	A:SER302	4.6	21.2	1.0
	C11	A:AW8402	4.6	55.0	1.0
	C	A:LEU300	4.8	15.6	1.0
	O	A:HOH854	4.8	37.8	1.0

Reference:

I.Crespo, J.Gimenez-Dejoz, S.Porte, A.Cousido-Siah, A.Mitschler, A.Podjarny, H.Pratsinis, D.Kletsas, X.Pares, F.X.Ruiz, K.Metwally, J.Farres. Design, Synthesis, Structure-Activity Relationships and X-Ray Structural Studies of Novel 1-Oxopyrimido[4,5-C]Quinoline-2-Acetic Acid Derivatives As Selective and Potent Inhibitors of Human Aldose Reductase. Eur J Med Chem V. 152 160 2018.
ISSN: ISSN 1768-3254
PubMed: 29705708
DOI: 10.1016/J.EJMECH.2018.04.015

Page generated: Fri Jul 26 14:54:15 2024

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