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1bkw

;p-Hydroxybenzoate hydroxylase (phbh) mutant with cys116 replaced by ser (c116s) and arg44 replaced by lys (r44k), in complex with fad and 4-hydroxybenzoic acid ;

Method: X-RAY DIFFRACTION D_max: 71.8 Å Quality: GOOD

SAXS Profile

P(r) Distribution

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1. Structure Basics

entry_id	1bkw
deposition_date	1998-07-13
title	;p-Hydroxybenzoate hydroxylase (phbh) mutant with cys116 replaced by ser (c116s) and arg44 replaced by lys (r44k), in complex with fad and 4-hydroxybenzoic acid ;
keywords	HYDROXYBENZOATE, 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	22.58 Å
rg_electron	21.53 Å
i0	34371200.00
molecular_weight	44812.0 kDa
excluded_volume	55953 Å³
envelope_volume	64971 Å³
shell_volume	24878 Å³
envelope_diameter	72.7 Å
shell_rg	28.63 Å
envelope_rg	21.77 Å
shape_rg	21.53 Å
total_rg	22.35 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	71.8 Å
rg_real	22.53 Å
rg_real_error	0.38 Å
i0_real	3.4370e+07
i0_real_error	4.5370e+05
rg_reciprocal	22.54 Å
i0_reciprocal	34370000.0000
total_estimate	0.8966
solution_quality	GOOD a GOOD solution
n_peaks	2
r_peak_primary	26.1 Å
skewness	0.308
kurtosis	-0.371
angular_range	— – 0.3500 Å⁻¹
current_alpha	0.0000
highest_alpha	11090000.0000
n_real_points	67
gnom_version	4.1.3
quality_criteria	AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.995

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4. Crystallography & Experiment

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5. Entities & Polymer Info (4)

Entity 1 polymer

description	PROTEIN (P-HYDROXYBENZOATE HYDROXYLASE)
formula_weight	44336.5 kDa
ec_number	1.14.13.2
mutation	R44K, C116S
src_method	man
entity_count	1

Polymer

type	polypeptide(L)
strand_id	A
atom_count	3402

MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIKAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREASGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE

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	243

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6. Citations (10)

Structure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding.

Eur.J.Biochem. (1995)

PMID: 7628466 · DOI: 10.1111/j.1432-1033.1995.0157f.x PRIMARY

;Crystal Structure of P-Hydroxybenzoate Hydroxylase Reconstituted with the Modified FAD Present in Alcohol Oxidase from Methyloprophic 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 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 Angstroms Resolution

Proteins (1992)

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

FEBS Lett. (1990)

;Crystal Structure of the P-Hydroxybenzoate Hydroxylase-Substrate Complex Refined at 1.9 Angstroms 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	72.700 Å
length_b	146.400 Å
length_c	88.500 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	0.1820
r_work	0.1820
r_free	—

fit	/app/data/saxs_computation/bk/1bkw/1bkw.fit
pddf	/app/data/pr_computation/bk/1bkw/1bkw.pr.out
profile	/app/data/saxs_computation/bk/1bkw/1bkw.dat

;p-Hydroxybenzoate hydroxylase (phbh) mutant with cys116 replaced by ser (c116s) and arg44 replaced by lys (r44k), 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