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1axe

;CRYSTAL STRUCTURE OF THE ACTIVE-SITE MUTANT PHE93->TRP OF HORSE LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH NAD AND INHIBITOR TRIFLUOROETHANOL ;

Method: X-RAY DIFFRACTION D_max: 104.7 Å Quality: GOOD

SAXS Profile

P(r) Distribution

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1. Structure Basics

entry_id	1axe
deposition_date	1997-10-15
title	;CRYSTAL STRUCTURE OF THE ACTIVE-SITE MUTANT PHE93->TRP OF HORSE LIVER ALCOHOL DEHYDROGENASE IN COMPLEX WITH NAD AND INHIBITOR TRIFLUOROETHANOL ;
keywords	OXIDOREDUCTASE (NAD(A)-CHOH(D)), ALCOHOL DEHYDROGENASE, OXIDOREDUCTASE; OXIDOREDUCTASE
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	29.79 Å
rg_electron	29.71 Å
i0	105168000.00
molecular_weight	81483.0 kDa
excluded_volume	102100 Å³
envelope_volume	119260 Å³
shell_volume	34282 Å³
envelope_diameter	109.8 Å
shell_rg	36.13 Å
envelope_rg	29.91 Å
shape_rg	29.73 Å
total_rg	30.21 Å
total_atoms	5680
n_residues	748
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	104.7 Å
rg_real	29.94 Å
rg_real_error	0.95 Å
i0_real	1.0520e+08
i0_real_error	1.8100e+06
rg_reciprocal	29.88 Å
i0_reciprocal	105200000.0000
total_estimate	0.8455
solution_quality	GOOD a GOOD solution
n_peaks	2
r_peak_primary	29.6 Å
skewness	0.499
kurtosis	-0.275
angular_range	— – 0.2650 Å⁻¹
current_alpha	0.0000
highest_alpha	51960000.0000
n_real_points	54
gnom_version	4.1.3
quality_criteria	AN1: 0.000; Oscil: 0.725; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.857; Smooth: 0.954

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4. Crystallography & Experiment

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5. Entities & Polymer Info (5)

Entity 1 polymer

description	ALCOHOL DEHYDROGENASE
formula_weight	39892.3 kDa
ec_number	1.1.1.1
mutation	F93W
src_method	man
entity_count	2

Polymer

type	polypeptide(L)
strand_id	A,B
atom_count	5796

STAGKVIKCKAAVLWEEKKPFSIEEVEVAPPKAHEVRIKMVATGICRSDDHVVSGTLVTPLPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLWTPQCGKCRVCKHPEGNFCLKNDLSMPRGTMQDGTSRFTCRGKPIHHFLGTSTFSQYTVVDEISVAKIDAASPLEKVCLIGCGFSTGYGSAVKVAKVTQGSTCAVFGLGGVGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATECVNPQDYKKPIQEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQNLSMNPMLLLSGRTWKGAIFGGFKSKDSVPKLVADFMAKKFALDPLITHVLPFEKINEGFDLLRSGESIRTILTF

Source

organism	Equus caballus
common_name	horse
ncbi_taxonomy_id	9796
host_organism	Escherichia coli

Entity 2 non-polymer

description	ZINC ION
formula_weight	65.4 kDa
src_method	syn
entity_count	4

Entity 3 non-polymer

description	NICOTINAMIDE-ADENINE-DINUCLEOTIDE
formula_weight	663.4 kDa
src_method	syn
entity_count	2

Entity 4 non-polymer

description	TRIFLUOROETHANOL
formula_weight	100.0 kDa
src_method	syn
entity_count	2

Entity 5 water

description	water
formula_weight	18.0 kDa
src_method	nat
entity_count	116

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6. Citations (12)

A link between protein structure and enzyme catalyzed hydrogen tunneling.

Proc.Natl.Acad.Sci.USA (1997)

PMID: 9371755 · DOI: 10.1073/pnas.94.24.12797 PRIMARY

Refined Crystal Structure of Liver Alcohol Dehydrogenase-Nadh Complex at 1.8 A Resolution

Acta Crystallogr.,Sect.D (1994)

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)

;Crystal-Structure Determination of Reduced Nicotinamide Adenine Dinucleotide Complex with Horse Liver Alcohol Dehydrogenase Maintained in its Apo Conformation by Zinc-Bound Imidazole ;

Biochemistry (1983)

Three-Dimensional Structure of Isonicotinimidylated Liver Alcohol Dehydrogenase

J.Biol.Chem. (1983)

;Crystal Structures of the Active Site in Specifically Metal-Depleted and Cobalt-Substituted Horse Liver Alcohol Dehydrogenase Derivatives ;

Proc.Natl.Acad.Sci.USA (1983)

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)

Structural Differences between Apo-and Holoenzyme of Horse Liver Alcohol Dehydrogenase

J.Biol.Chem. (1979)

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

J.Mol.Biol. (1976)

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length_a	51.820 Å
length_b	44.580 Å
length_c	93.280 Å
angle_alpha	103.10 °
angle_beta	87.59 °
angle_gamma	70.55 °
z_pdb	2

space_group	P 1
int_tables_number	1
crystal_system	—

resolution	2.000 Å
resolution_low	10.000 Å
r_factor	0.2030
r_work	0.2030
r_free	0.2690

fit	/app/data/saxs_computation/ax/1axe/1axe.fit
pddf	/app/data/pr_computation/ax/1axe/1axe.pr.out
profile	/app/data/saxs_computation/ax/1axe/1axe.dat