SAXSdb — 1pbb

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1. Protein Identity and Related Structures Protein Identity & Related Structures

P-HYDROXYBENZOATE HYDROXYLASE

Pseudomonas fluorescens

State in the Current Structure

Assembly	Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Associated Components	Method and Experimental Conditions	Structure Quality
1	Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count	Chain A； UniProt 1–394	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 DOB 2,4-DIHYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.50 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

Other PDB	Difference from Current Entry 1PBB	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
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 Deposited 1998-05-26	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–394（394 aa）	Mutation：R42K, C116S	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 30 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	Resolution 2.20 Å
1BGJ P-HYDROXYBENZOATE HYDROXYLASE (PHBH) MUTANT WITH CYS 116 REPLACED BY SER (C116S) AND HIS 162 REPLACED BY ARG (H162R), IN COMPLEX WITH FAD AND 4-HYDROXYBENZOIC ACID Deposited 1998-05-29	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–394（394 aa）	Mutation：C116S, H162R	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 30 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	Resolution 3.00 Å
1BGN P-HYDROXYBENZOATE HYDROXYLASE (PHBH) MUTANT WITH CYS 116 REPLACED BY SER (C116S) AND ARG 269 REPLACED BY THR (R269T), IN COMPLEX WITH FAD AND 4-HYDROXYBENZOIC ACID Deposited 1998-05-29	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–394（394 aa）	Mutation：C116S, R269T	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 30 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	Resolution 2.00 Å
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 Deposited 1998-07-13	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–394（394 aa）	Mutation：R44K, C116S	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 PHB P-HYDROXYBENZOIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	Resolution 2.20 Å
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 Deposited 1998-07-13	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–394（394 aa）	Mutation：R44K, C116S	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	Resolution 2.20 Å
1CC4 PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY. Deposited 1999-03-04	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–394（394 aa）	Mutation：F161A, C116S	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 PHB P-HYDROXYBENZOIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7.0	Resolution 2.00 Å
1CC4 PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY. Deposited 1999-03-04	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–394（394 aa）	Mutation：F161A, C116S	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7.0	Resolution 2.00 Å
1CC6 PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY. Deposited 1999-03-04	Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–394（394 aa）	Mutation：R166S, C116S	FAD FLAVIN-ADENINE DINUCLEOTIDE × 1 PHB P-HYDROXYBENZOIC ACID × 1	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；pH 7.0	Resolution 2.20 Å
1CJ2 MUTANT GLN34ARG OF PARA-HYDROXYBENZOATE HYDROXYLASE Deposited 1999-04-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–391（391 aa）	Mutation：Q34R	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	Resolution 2.80 Å
1CJ2 MUTANT GLN34ARG OF PARA-HYDROXYBENZOATE HYDROXYLASE Deposited 1999-04-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–391（391 aa）	Mutation：Q34R	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；39% AMMONIUMSULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	Resolution 2.80 Å
1CJ3 MUTANT TYR38GLU OF PARA-HYDROXYBENZOATE HYDROXYLASE Deposited 1999-04-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–392（392 aa）	Mutation：Y38E	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；39% AMMONIUM SULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	Resolution 2.50 Å
1CJ3 MUTANT TYR38GLU OF PARA-HYDROXYBENZOATE HYDROXYLASE Deposited 1999-04-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–392（392 aa）	Mutation：Y38E	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；39% AMMONIUM SULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	Resolution 2.50 Å
1CJ4 MUTANT Q34T OF PARA-HYDROXYBENZOATE HYDROXYLASE Deposited 1999-04-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–392（392 aa）	Mutation：Q34T	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；39% AMMONIUM SULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	Resolution 2.40 Å
1CJ4 MUTANT Q34T OF PARA-HYDROXYBENZOATE HYDROXYLASE Deposited 1999-04-21	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–392（392 aa）	Mutation：Q34T	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7；39% AMMONIUM SULFATE, 100 MM SODIUM PHOSPHATE, 0.04 MM FAD, 0.15 MM EDTA, 60 MM SODIUM SULFITE, 1 MM P-HYDROXYBENZOATE, pH 7.0	Resolution 2.40 Å
1PBC CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4-DIHYDROXYBENZOATE AND 2-HYDROXY-4-AMINOBENZOATE AND OF THE TRY222ALA MUTANT, COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING Deposited 1994-07-06	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–394（394 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 BHA 2-HYDROXY-4-AMINOBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.80 Å
1PBD CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4-DIHYDROXYBENZOATE AND 2-HYDROXY-4-AMINOBENZOATE AND OF THE TRY222ALA MUTANT, COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING Deposited 1994-07-06	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–394（394 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PAB 4-AMINOBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
1PBE CRYSTAL STRUCTURE OF THE P-HYDROXYBENZOATE HYDROXYLASE-SUBSTRATE COMPLEX REFINED AT 1.9 ANGSTROMS RESOLUTION. ANALYSIS OF THE ENZYME-SUBSTRATE AND ENZYME-PRODUCT COMPLEXES Deposited 1994-07-06	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–394（394 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.90 Å
1PBF CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4-DIHYDROXYBENZOATE AND 2-HYDROXY-4-AMINOBENZOATE AND OF THE TRY222ALA MUTANT, COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING Deposited 1994-07-06	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–394（394 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 BHA 2-HYDROXY-4-AMINOBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å
1PDH CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE RECONSTITUTED WITH THE MODIFIED FAD PRESENT IN ALCOHOL OXIDASE FROM METHYLOTROPHIC YEASTS: EVIDENCE FOR AN ARABINOFLAVIN Deposited 1994-12-01	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–394（394 aa）	Not recorded	FAS ARABINO-FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å
1PHH CRYSTAL STRUCTURE OF P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH ITS REACTION PRODUCT 3,4-DIHYDROXYBENZOATE Deposited 1987-11-04	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–394（394 aa）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 DHB 3,4-DIHYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
2PHH THE COENZYME ANALOGUE ADENOSINE 5-DIPHOSPHORIBOSE DISPLACES FAD IN THE ACTIVE SITE OF P-HYDROXYBENZOATE HYDROXYLASE. AN X-RAY CRYSTALLOGRAPHIC INVESTIGATION Deposited 1989-06-19	Different ligand/ion Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 1–394（394 aa）	Not recorded	APR ADENOSINE-5-DIPHOSPHORIBOSE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.70 Å

16 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PHHY_PSEFL
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–394； UniProt 1–394

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1pbb
Deposition date deposition_date	1994-07-06
Structure title title	CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4-DIHYDROXYBENZOATE AND 2-HYDROXY-4-AMINOBENZOATE AND OF THE TRY222ALA MUTANT, COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING
Keywords keywords	OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method method	X-RAY DIFFRACTION

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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier	22.57 Å
Radius of gyration Rg (electron density) rg_electron	21.55 Å
Forward intensity I(0) i0	34701500.00
Molecular weight molecular_weight	44856.0 kDa
Excluded volume excluded_volume	55967 Å³
Envelope volume envelope_volume	65277 Å³
Hydration-shell volume shell_volume	25004 Å³
Envelope diameter envelope_diameter	72.3 Å
Shell Rg shell_rg	28.56 Å
Envelope Rg envelope_rg	21.74 Å
Shape Rg shape_rg	21.56 Å
Total Rg total_rg	22.38 Å
Total atoms total_atoms	3162
Residues n_residues	391
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	70.5 Å
Rg (real space) rg_real	22.52 Å
Rg uncertainty (real space) rg_real_error	0.31 Å
I(0) (real space) i0_real	3.4700e+07
I(0) uncertainty (real space) i0_real_error	3.9370e+05
Rg (reciprocal space) rg_reciprocal	22.53 Å
I(0) (reciprocal space) i0_reciprocal	34700000.0000
Solution quality estimate total_estimate	0.6994
Solution quality rating solution_quality	REASONABLE a REASONABLE solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	69.5 Å
Skewness Skewness skewness	0.304
Kurtosis Kurtosis kurtosis	-0.378
Angular range angular_range	— – 0.3500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	11430000.0000
Real-space data points n_real_points	67
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.907; Stabil: 1.000; Sysdev: 0.130; Positv: 1.000; Valcen: 0.998; Smooth: 0.979

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

Entity 1 Entity 1 polymer

Description description	P-HYDROXYBENZOATE HYDROXYLASE
Molecular weight formula_weight	44364.5 kDa
EC 编号 ec_number	1.14.13.2
Source method src_method	man
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	3365

MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREASGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE

来源 Source

来源生物 organism	Pseudomonas fluorescens
NCBI Class编号 ncbi_taxonomy_id	294

Entity 2 Entity 2 non-polymer

Description description	FLAVIN-ADENINE DINUCLEOTIDE
Molecular weight formula_weight	785.5 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 3 Entity 3 non-polymer

Description description	2,4-DIHYDROXYBENZOIC ACID
Molecular weight formula_weight	154.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 4 Entity 4 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	203

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1pbba1
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.3 — FAD/NAD(P)-binding domain
Superfamily Superfamily superfamily	c.3.1 — FAD/NAD(P)-binding domain
Family Family family	c.3.1.2 — FAD-linked reductases, N-terminal domain

Domain ID domain_id	d1pbba2
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.16 — FAD-linked reductases, C-terminal domain
Superfamily Superfamily superfamily	d.16.1 — FAD-linked reductases, C-terminal domain
Family Family family	d.16.1.2 — PHBH-like

CATH v4.4 (2 domains)

Domain ID domain_id	1pbbA01
Class class	3 — Alpha Beta
Architecture architecture	50 — 3-Layer(bba) Sandwich
Topology topology	50 — FAD/NAD(P)-binding domain
Homologous superfamily homologous superfamily	60 — FAD/NAD(P)-binding domain

Domain ID domain_id	1pbbA02
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	9 — D-Amino Acid Oxidase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — D-Amino Acid Oxidase, subunit A, domain 2

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8. Citations (11)

;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)

PMID: 7520279 · DOI: 10.1021/bi00199a044 PRIMARY

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

Proteins (1992)

The Influence of Purification and Protein Heterogeneity on the Crystallization of P-Hydroxybenzoate Hydroxylase

Eur.J.Biochem. (1989)

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

Biochemistry (1989)

Analysis of the Active Site of the Flavoprotein P-Hydroxybenzoate Hydroxylase and Some Ideas with Respect to its Reaction Mechanism

Biochemistry (1989)

;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)

;Molecular Modeling Reveals the Possible Importance of a Carbonyl Oxygen Binding Pocket for the Catalytic Mechanism of P-Hydroxybenzoate Hydroxylase ;

J.Biol.Chem. (1988)

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

J.Mol.Biol. (1988)

;Comparison of the Three-Dimensional Protein and Nucleotide Structure of the Fad-Binding Domain of P-Hydroxybenzoate Hydroxylase with the Fad-as Well as Nadph-Binding Domains of Glutathione Reductase ;

J.Mol.Biol. (1983)

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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Unit-cell length a length_a	72.300 Å
Unit-cell length b length_b	146.200 Å
Unit-cell length c length_c	89.000 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	8

Space group space_group	C 2 2 21
Space-group number int_tables_number	20
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	8.000 Å
R factor r_factor	0.1580
R_work r_work	0.1580
R_free r_free	—

fit	/app/data/saxs_computation/pb/1pbb/1pbb.fit
pddf	/app/data/pr_computation/pb/1pbb/1pbb.pr.out
profile	/app/data/saxs_computation/pb/1pbb/1pbb.dat

CRYSTAL STRUCTURES OF WILD-TYPE P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE, 2,4-DIHYDROXYBENZOATE AND 2-HYDROXY-4-AMINOBENZOATE AND OF THE TRY222ALA MUTANT, COMPLEXED WITH 2-HYDROXY-4-AMINOBENZOATE. EVIDENCE FOR A PROTON CHANNEL AND A NEW BINDING MODE OF THE FLAVIN RING