← Back to search

1axg

;CRYSTAL STRUCTURE OF THE VAL203->ALA MUTANT OF LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH COFACTOR NAD AND INHIBITOR TRIFLUOROETHANOL SOLVED TO 2.5 ANGSTROM RESOLUTION ;

Method: X-RAY DIFFRACTION D_max: 117.8 Å Quality: EXCELLENT

SAXS Profile

P(r) Distribution

▼

1. Structure Basics

entry_id	1axg
deposition_date	1997-10-15
title	;CRYSTAL STRUCTURE OF THE VAL203->ALA MUTANT OF LIVER ALCOHOL DEHYDROGENASE COMPLEXED WITH COFACTOR NAD AND INHIBITOR TRIFLUOROETHANOL SOLVED TO 2.5 ANGSTROM RESOLUTION ;
keywords	OXIDOREDUCTASE (NAD(A)-CHOH(D)), ALCOHOL DEHYDROGENASE, OXIDOREDUCTASE; OXIDOREDUCTASE
method	X-RAY DIFFRACTION

▼

Download Data

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

▼

2. SAXS Parameters (CRYSOL)

rg_guinier	36.85 Å
rg_electron	36.57 Å
i0	398743000.00
molecular_weight	162700.0 kDa
excluded_volume	203810 Å³
envelope_volume	246430 Å³
shell_volume	55045 Å³
envelope_diameter	121.0 Å
shell_rg	43.65 Å
envelope_rg	36.14 Å
shape_rg	36.59 Å
total_rg	36.94 Å
total_atoms	11340
n_residues	1496
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

▼

3. P(r) Analysis (GNOM)

dmax	117.8 Å
rg_real	36.71 Å
rg_real_error	0.88 Å
i0_real	3.9870e+08
i0_real_error	7.0290e+06
rg_reciprocal	36.80 Å
i0_reciprocal	398800000.0000
total_estimate	0.9027
solution_quality	EXCELLENT a EXCELLENT solution
n_peaks	1
r_peak_primary	49.3 Å
skewness	0.163
kurtosis	-0.567
angular_range	— – 0.2150 Å⁻¹
current_alpha	0.0000
highest_alpha	92680000.0000
n_real_points	44
gnom_version	4.1.3
quality_criteria	AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.935

▶

4. Crystallography & Experiment

▶

5. Entities & Polymer Info (5)

Entity 1 polymer

description	ALCOHOL DEHYDROGENASE
formula_weight	39825.2 kDa
ec_number	1.1.1.1
mutation	V203A
src_method	man
entity_count	4

Polymer

type	polypeptide(L)
strand_id	A,B,C,D
atom_count	11655

STAGKVIKCKAAVLWEEKKPFSIEEVEVAPPKAHEVRIKMVATGICRSDDHVVSGTLVTPLPVIAGHEAAGIVESIGEGVTTVRPGDKVIPLFTPQCGKCRVCKHPEGNFCLKNDLSMPRGTMQDGTSRFTCRGKPIHHFLGTSTFSQYTVVDEISVAKIDAASPLEKVCLIGCGFSTGYGSAVKVAKVTQGSTCAVFGLGGAGLSVIMGCKAAGAARIIGVDINKDKFAKAKEVGATECVNPQDYKKPIQEVLTEMSNGGVDFSFEVIGRLDTMVTALSCCQEAYGVSVIVGVPPDSQNLSMNPMLLLSGRTWKGAIFGGFKSKDSVPKLVADFMAKKFALDPLITHVLPFEKINEGFDLLRSGESIRTILTF

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	8

Entity 3 non-polymer

description	NICOTINAMIDE-ADENINE-DINUCLEOTIDE
formula_weight	663.4 kDa
src_method	syn
entity_count	4

Entity 4 non-polymer

description	TRIFLUOROETHANOL
formula_weight	100.0 kDa
src_method	syn
entity_count	4

Entity 5 water

description	water
formula_weight	18.0 kDa
src_method	nat
entity_count	315

▶

6. Citations (22)

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)

Structure of a Triclinic Ternary Complex of Horse Liver Alcohol Dehydrogenase at 2.9 A Resolution

J.Mol.Biol. (1981)

;5-Methylnicotinamide-Adenine Dinucleotide. Kinetic Investigation with Major and Minor Isoenzymes of Liver Alcohol Dehydrogenase and Structural Determination of its Binary Complex with Alcohol Dehydrogenase ;

Eur.J.Biochem. (1981)

X-Ray Studies of the Binding of Cibacron Blue F3Ga to Liver Alcohol Dehydrogenase

Eur.J.Biochem. (1979)

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

J.Biol.Chem. (1979)

Subunit Conformation of Yeast Alcohol Dehydrogenase

J.Biol.Chem. (1978)

Crystallization of Liver Alcohol Dehydrogenase Activated by the Modification of Amino Groups

J.Mol.Biol. (1978)

Crystallography of Liver Alcohol Dehydrogenase Complexed with Substrates

J.Mol.Biol. (1978)

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

Eur.J.Biochem. (1977)

;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)

Structural Comparisons of Mammalian, Yeast and Bacillar Alcohol Dehydrogenases

J.Mol.Biol. (1976)

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

J.Mol.Biol. (1976)

The Binding of Nucleotides to Horse Liver Alcohol

;STRUCTURE AND CONFORMATION OF NUCLEIC ACIDS AND PROTEIN-NUCLEIC ACID INTERACTIONS : PROCEEDINGS OF THE FOURTH ANNUAL HARRY STEENBOCK SYMPOSIUM, JUNE 16-19, 1974, MADISON, WISCONSIN ; (1975)

▶

length_a	44.348 Å
length_b	86.734 Å
length_c	90.635 Å
angle_alpha	102.66 °
angle_beta	99.24 °
angle_gamma	101.63 °
z_pdb	4

space_group	P 1
int_tables_number	1
crystal_system	—

resolution	2.500 Å
resolution_low	10.000 Å
r_factor	0.2140
r_work	0.2140
r_free	0.2940

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