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1bf3

;P-HYDROXYBENZOATE HYDROXYLASE (PHBH) MUTANT WITH CYS 116 REPLACED BY SER (C116S) AND ARG 42 REPLACED BY LYS (R42K), IN COMPLEX WITH FAD AND 4-HYDROXYBENZOIC ACID ;

Method: X-RAY DIFFRACTION D_max: 71.7 Å Quality: GOOD

SAXS Profile

P(r) Distribution

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1. Structure Basics

entry_id	1bf3
deposition_date	1998-05-26
title	;P-HYDROXYBENZOATE HYDROXYLASE (PHBH) MUTANT WITH CYS 116 REPLACED BY SER (C116S) AND ARG 42 REPLACED BY LYS (R42K), IN COMPLEX WITH FAD AND 4-HYDROXYBENZOIC ACID ;
keywords	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	22.55 Å
rg_electron	21.53 Å
i0	34384700.00
molecular_weight	44812.0 kDa
excluded_volume	55953 Å³
envelope_volume	64761 Å³
shell_volume	24829 Å³
envelope_diameter	73.9 Å
shell_rg	28.53 Å
envelope_rg	21.76 Å
shape_rg	21.53 Å
total_rg	22.34 Å
total_atoms	3159
n_residues	391
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	71.7 Å
rg_real	22.50 Å
rg_real_error	0.35 Å
i0_real	3.4380e+07
i0_real_error	4.5710e+05
rg_reciprocal	22.51 Å
i0_reciprocal	34380000.0000
total_estimate	0.8965
solution_quality	GOOD a GOOD solution
n_peaks	2
r_peak_primary	26.1 Å
skewness	0.314
kurtosis	-0.364
angular_range	— – 0.3500 Å⁻¹
current_alpha	0.0000
highest_alpha	11580000.0000
n_real_points	67
gnom_version	4.1.3
quality_criteria	AN1: 0.000; Oscil: 0.885; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.996

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4. Crystallography & Experiment

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5. Entities & Polymer Info (4)

Entity 1 polymer

description	P-HYDROXYBENZOATE HYDROXYLASE
formula_weight	44336.5 kDa
ec_number	1.14.13.2
mutation	R42K, C116S
src_method	man
entity_count	1

Polymer

type	polypeptide(L)
strand_id	A
atom_count	3448

MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGKIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREASGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE

Source

organism	Pseudomonas fluorescens
ncbi_taxonomy_id	294
host_organism	Escherichia coli

Entity 2 non-polymer

description	FLAVIN-ADENINE DINUCLEOTIDE
formula_weight	785.5 kDa
src_method	syn
entity_count	1

Entity 3 non-polymer

description	P-HYDROXYBENZOIC ACID
formula_weight	138.1 kDa
src_method	syn
entity_count	1

Entity 4 water

description	water
formula_weight	18.0 kDa
src_method	nat
entity_count	289

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6. Citations (10)

;Lys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding. ;

Eur.J.Biochem. (1998)

PMID: 9578477 · DOI: 10.1046/j.1432-1327.1998.2530194.x PRIMARY

;Crystal Structure of P-Hydroxybenzoate Hydroxylase Reconstituted with the Modified Fad Present in Alcohol Oxidase from Methylotrophic Yeasts: Evidence for an Arabinoflavin ;

Protein Sci. (1994)

;Crystal Structures of Wild-Type P-Hydroxybenzoate Hydroxylase Complexed with 4-Aminobenzoate, 2,4-Dihydroxybenzoate, and 2-Hydroxy-4-Aminobenzoate and of the Tyr222Ala Mutant Complexed with 2-Hydroxy-4-Aminobenzoate. Evidence for a Proton Channel and a New Binding Mode of the Flavin Ring ;

Biochemistry (1994)

Crystal Structure of the Reduced Form of P-Hydroxybenzoate Hydroxylase Refined at 2.3 A Resolution

Proteins (1992)

Engineering of Microheterogeneity-Resistant P-Hydroxybenzoate Hydroxylase from Pseudomonas Fluorescens

FEBS Lett. (1990)

;Crystal Structure of the P-Hydroxybenzoate Hydroxylase-Substrate Complex Refined at 1.9 A Resolution. Analysis of the Enzyme-Substrate and Enzyme-Product Complexes ;

J.Mol.Biol. (1989)

;The Coenzyme Analogue Adenosine 5-Diphosphoribose Displaces Fad in the Active Site of P-Hydroxybenzoate Hydroxylase. An X-Ray Crystallographic Investigation ;

Biochemistry (1989)

Crystal Structure of P-Hydroxybenzoate Hydroxylase Complexed with its Reaction Product 3,4-Dihydroxybenzoate

J.Mol.Biol. (1988)

Crystal Structure of P-Hydroxybenzoate Hydroxylase

J.Mol.Biol. (1979)

Crystallization and Preliminary X-Ray Investigation of P-Hydroxybenzoate Hydroxylase from Pseudomonas Fluorescens

J.Biol.Chem. (1975)

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length_a	71.350 Å
length_b	145.900 Å
length_c	88.800 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	2.200 Å
resolution_low	8.000 Å
r_factor	—
r_work	0.1750
r_free	—

fit	/app/data/saxs_computation/bf/1bf3/1bf3.fit
pddf	/app/data/pr_computation/bf/1bf3/1bf3.pr.out
profile	/app/data/saxs_computation/bf/1bf3/1bf3.dat

;P-HYDROXYBENZOATE HYDROXYLASE (PHBH) MUTANT WITH CYS 116 REPLACED BY SER (C116S) AND ARG 42 REPLACED BY LYS (R42K), IN COMPLEX WITH FAD AND 4-HYDROXYBENZOIC ACID ;

SAXS Profile

P(r) Distribution

1. Structure Basics

Download Data

2. SAXS Parameters (CRYSOL)

3. P(r) Analysis (GNOM)

4. Crystallography & Experiment

Unit Cell

Symmetry

Refinement

Diffraction