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1adg

;CRYSTALLOGRAPHIC STUDIES OF TWO ALCOHOL DEHYDROGENASE-BOUND ANALOGS OF THIAZOLE-4-CARBOXAMIDE ADENINE DINUCLEOTIDE (TAD), THE ACTIVE ANABOLITE OF THE ANTITUMOR AGENT TIAZOFURIN ;

Method: X-RAY DIFFRACTION D_max: 74.3 Å Quality: GOOD

SAXS Profile

P(r) Distribution

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1. Structure Basics

entry_id	1adg
deposition_date	1993-10-18
title	;CRYSTALLOGRAPHIC STUDIES OF TWO ALCOHOL DEHYDROGENASE-BOUND ANALOGS OF THIAZOLE-4-CARBOXAMIDE ADENINE DINUCLEOTIDE (TAD), THE ACTIVE ANABOLITE OF THE ANTITUMOR AGENT TIAZOFURIN ;
keywords	OXIDOREDUCTASE(NAD(A)-CHOH(D)); OXIDOREDUCTASE(NAD(A)-CHOH(D))
method	X-RAY DIFFRACTION

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Download Data

SAXS curve (.dat) P(r) distribution (.pr.out) Structure (CIF)

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2. SAXS Parameters (CRYSOL)

rg_guinier	21.67 Å
rg_electron	20.84 Å
i0	28015700.00
molecular_weight	40654.0 kDa
excluded_volume	50912 Å³
envelope_volume	57789 Å³
shell_volume	23111 Å³
envelope_diameter	76.4 Å
shell_rg	27.66 Å
envelope_rg	21.12 Å
shape_rg	20.83 Å
total_rg	21.68 Å
total_atoms	3445
n_residues	374
n_harmonics	20
q_range	— – 0.5000 Å⁻¹
n_points	101
shell_type	directional
solvent_density	0.3340 e/Å³
contrast_shell	0.0300 e/Å³
crysol_version	4.1.3

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3. P(r) Analysis (GNOM)

dmax	74.3 Å
rg_real	21.64 Å
rg_real_error	0.42 Å
i0_real	2.8020e+07
i0_real_error	3.2830e+05
rg_reciprocal	21.65 Å
i0_reciprocal	28020000.0000
total_estimate	0.8661
solution_quality	GOOD a GOOD solution
n_peaks	2
r_peak_primary	25.5 Å
skewness	0.366
kurtosis	-0.223
angular_range	— – 0.3650 Å⁻¹
current_alpha	0.0000
highest_alpha	8019000.0000
n_real_points	68
gnom_version	4.1.3
quality_criteria	AN1: 0.000; Oscil: 0.768; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.980

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4. Crystallography & Experiment

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5. Entities & Polymer Info (4)

Entity 1 polymer

description	ALCOHOL DEHYDROGENASE
formula_weight	39853.3 kDa
ec_number	1.1.1.1
src_method	man
entity_count	1

Polymer

type	polypeptide(L)
strand_id	A
atom_count	3601

STAGKVIKCKAAVLWEEKKPFSIEEVEVAPPKAHEVRIKMVATGICRSDDHVVSGTLVTPLPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLFTPQCGKCRVCKHPEGNFCLKNDLSMPRGTMQDGTSRFTCRGKPIHHFLGTSTFSQYTVVDEISVAKIDAASPLEKVCLIGCGFSTGYGSAVKVAKVTQGSTCAVFGLGGVGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATECVNPQDYKKPIQEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQNLSMNPMLLLSGRTWKGAIFGGFKSKDSVPKLVADFMAKKFALDPLITHVLPFEKINEGFDLLRSGESIRTILTF

Source

organism	Equus caballus
common_name	horse
ncbi_taxonomy_id	9796

Entity 2 non-polymer

description	ZINC ION
formula_weight	65.4 kDa
src_method	syn
entity_count	2

Entity 3 non-polymer

description	BETA-METHYLENE-SELENAZOLE-4-CARBOXYAMIDE-ADENINE DINUCLEOTIDE
formula_weight	714.4 kDa
src_method	syn
entity_count	1

Entity 4 water

description	water
formula_weight	18.0 kDa
src_method	nat
entity_count	52

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6. Citations (15)

;Crystallographic studies of two alcohol dehydrogenase-bound analogues of thiazole-4-carboxamide adenine dinucleotide (TAD), the active anabolite of the antitumor agent tiazofurin. ;

Biochemistry (1994)

PMID: 8286346 · DOI: 10.1021/bi00167a004 PRIMARY

Interdomain Motion in Liver Alcohol Dehydrogenase. Structural and Energetic Analysis of the Hinge Bending Mode

J.Biol.Chem. (1986)

Crystallographic Investigations of Nicotinamide Adenine Dinucleotide Binding to Horse Liver Alcohol Dehydrogenase

Biochemistry (1984)

Pyrazole Binding in Crystalline Binary and Ternary Complexes with Liver Alcohol Dehydrogenase

Biochemistry (1982)

;Crystal Structure Determinations of Coenzyme Analogue and Substrate Complexes of Liver Alcohol Dehydrogenase. Binding of 1,4,5,6-Tetrahydronicotinamide Adenine Dinucleotide and Trans-4-(N,N-Dimethylamino)Cinnamaldehyde to the Enzyme ;

Biochemistry (1982)

Binding of Substrate in a Ternary Complex of Horse Liver Alcohol Dehydrogenase

J.Biol.Chem. (1982)

Subunit Conformation of Yeast Alcohol Dehydrogenase

J.Biol.Chem. (1978)

;The Crystal Structure of Complexes between Horse Liver Alcohol Dehydrogenase and the Coenzyme Analogues 3-Iodopyridine-Adenine Dinucleotide and Pyridine-Adenine Dinucleotide ;

Eur.J.Biochem. (1977)

X-Ray Investigation of the Binding of 1,10-Phenanthroline and Imidazole to Horse-Liver Alcohol Dehydrogenase

Eur.J.Biochem. (1977)

Three-Dimensional Structure of Horse Liver Alcohol Dehydrogenase at 2.4 Angstroms Resolution

J.Mol.Biol. (1976)

Alcohol Dehydrogenases

The Enzymes,Third Edition (1975)

The Conformation of Adenosine Diphosphoribose and 8-Bromoadenosine Diphosphoribose When Bound to Liver Alcohol Dehydrogenase

Eur.J.Biochem. (1975)

Structural and Functional Similarities within the Coenzyme Binding Domains of Dehydrogenases

J.Mol.Biol. (1974)

Binding of Salicylate in the Adenosine-Binding Pocket of Dehydrogenases

Eur.J.Biochem. (1974)

Untitled

Atlas of Protein Sequence and Structure (Data Section) (1972)

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length_a	56.300 Å
length_b	75.200 Å
length_c	182.300 Å
angle_alpha	90.00 °
angle_beta	90.00 °
angle_gamma	90.00 °
z_pdb	8

space_group	C 2 2 21
int_tables_number	20
crystal_system	—

resolution	2.700 Å
resolution_low	— Å
r_factor	0.1600
r_work	0.1600
r_free	—

fit	/app/data/saxs_computation/ad/1adg/1adg.fit
pddf	/app/data/pr_computation/ad/1adg/1adg.pr.out
profile	/app/data/saxs_computation/ad/1adg/1adg.dat