SAXSdb — 1ius

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

P-HYDROXYBENZOATE HYDROXYLASE

Pseudomonas aeruginosa

UniProt P20586

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 PAB 4-AMINOBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions：pH 5；pH 5.0	Resolution 2.20 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 1IUS	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1D7L STRUCTURE-FUNCTION CORRELATIONS OF THE REACTION OF REDUCED NICOTINAMIDE ANALOGS WITH P-HYDROXYBENZOATE HYDROXYLASE SUBSTITUTED WITH A SERIES OF 8-SUBSTITUTED FLAVINS Deposited 1999-10-18	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）	Not recorded	SO4 SULFATE ION × 3 RFL 8-DEMETHYL-8-DIMETHYLAMINO-FLAVIN-ADENINE-DINUCLEOTIDE × 1 PHB P-HYDROXYBENZOIC ACID × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å R-free 0.235
1D7L STRUCTURE-FUNCTION CORRELATIONS OF THE REACTION OF REDUCED NICOTINAMIDE ANALOGS WITH P-HYDROXYBENZOATE HYDROXYLASE SUBSTITUTED WITH A SERIES OF 8-SUBSTITUTED FLAVINS Deposited 1999-10-18	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）	Not recorded	SO4 SULFATE ION × 6 RFL 8-DEMETHYL-8-DIMETHYLAMINO-FLAVIN-ADENINE-DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å R-free 0.235
1DOB THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS Deposited 1994-09-06	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）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
1DOC THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS Deposited 1994-09-06	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）	Not recorded	BR BROMIDE ION × 6 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.00 Å
1DOD THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS Deposited 1994-09-06	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）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 DOB 2,4-DIHYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å
1DOE THE MOBIL FLAVIN OF 4-OH BENZOATE HYDROXYLASE: MOTION OF A PROSTHETIC GROUP REGULATES CATALYSIS Deposited 1994-09-06	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）	Not recorded	BR BROMIDE ION × 4 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 DOB 2,4-DIHYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
1IUT P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE AT PH 7.4 Deposited 1995-11-22	Different experimental conditions 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 X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.00 Å
1IUU P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE AT PH 9.4 Deposited 1995-11-22	Different experimental conditions 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 X-ray crystallization conditions pH 9.4；pH 9.4	Resolution 2.00 Å
1IUV P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE AT PH 5.0 Deposited 1995-11-22	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 X-ray crystallization conditions pH 5；pH 5.0	Resolution 2.50 Å
1IUW P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE AT PH 7.4 Deposited 1995-11-22	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）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.4；pH 7.4	Resolution 2.00 Å
1IUX P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-4-HYDROXYBENZOATE AT PH 9.4 Deposited 1995-11-22	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）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions pH 9.4；pH 9.4	Resolution 2.00 Å
1K0I Pseudomonas aeruginosa phbh R220Q in complex with 100mM PHB Deposited 2001-09-19	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：R220Q	SO4 SULFATE ION × 16 SO3 SULFITE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；303 K；100mM potassium phosphate, 0.05 mM glutathion, 30mM sodium sulfite 0.02mM FAD, 450mM ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 303K	Resolution 1.80 Å R-free 0.240
1K0I Pseudomonas aeruginosa phbh R220Q in complex with 100mM PHB Deposited 2001-09-19	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：R220Q	SO4 SULFATE ION × 16 SO3 SULFITE ION × 2 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；303 K；100mM potassium phosphate, 0.05 mM glutathion, 30mM sodium sulfite 0.02mM FAD, 450mM ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 303K	Resolution 1.80 Å R-free 0.240
1K0J Pseudomonas aeruginosa phbh R220Q in complex with NADPH and free of p-OHB Deposited 2001-09-19	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：R220Q	SO4 SULFATE ION × 10 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；303 K；100mM potassium phosphate, 0.05 mM glutathion, 30mM sodium sulfite 0.02mM FAD, 450mM ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 303K	Resolution 2.20 Å R-free 0.275
1K0J Pseudomonas aeruginosa phbh R220Q in complex with NADPH and free of p-OHB Deposited 2001-09-19	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：R220Q	SO4 SULFATE ION × 10 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；303 K；100mM potassium phosphate, 0.05 mM glutathion, 30mM sodium sulfite 0.02mM FAD, 450mM ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 303K	Resolution 2.20 Å R-free 0.275
1K0L Pseudomonas aeruginosa phbh R220Q free of p-OHB Deposited 2001-09-19	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：R220Q	SO4 SULFATE ION × 16 SO3 SULFITE ION × 4 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；303 K；100mM potassium phosphate, 0.05 mM glutathion, 30mM sodium sulfite 0.02mM FAD, 450mM ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 303K	Resolution 2.00 Å R-free 0.247
1K0L Pseudomonas aeruginosa phbh R220Q free of p-OHB Deposited 2001-09-19	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：R220Q	SO4 SULFATE ION × 16 SO3 SULFITE ION × 4 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；303 K；100mM potassium phosphate, 0.05 mM glutathion, 30mM sodium sulfite 0.02mM FAD, 450mM ammonium sulfate, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 303K	Resolution 2.00 Å R-free 0.247
1PXA CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZOATE HYDROXYLASE: THE TYR201PHE, TYR385PHE, AND ASN300ASP VARIANTS Deposited 1994-09-27	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）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
1PXB CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZOATE HYDROXYLASE: THE TYR201PHE, TYR385PHE, AND ASN300ASP VARIANTS Deposited 1994-09-27	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）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.30 Å
1PXC CRYSTAL STRUCTURES OF MUTANT PSEUDOMONAS AERUGINOSA P-HYDROXYBENZOATE HYDROXYLASE: THE TYR201PHE, TYR385PHE, AND ASN300ASP VARIANTS Deposited 1994-09-27	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）	Not recorded	FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.10 Å
1YKJ A45G p-hydroxybenzoate hydroxylase with p-hydroxybenzoate bound Deposited 2005-01-18	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 1–394（394 aa） Chain B 1–394（394 aa）	Mutation：A45G Mutation：A45G	SO4 SULFATE ION × 12 FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 PHB P-HYDROXYBENZOIC ACID × 2 PSL PYROSULFATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；310 K；ammonium sulfate, tris-sulfate, fad, edta, glutathion, sodium sulfite, p-hydroxybenzoate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 310K	Resolution 2.00 Å R-free 0.265
1YKJ A45G p-hydroxybenzoate hydroxylase with p-hydroxybenzoate bound Deposited 2005-01-18	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–394（394 aa） Chain B 1–394（394 aa）	Mutation：A45G Mutation：A45G	SO4 SULFATE ION × 24 FAD FLAVIN-ADENINE DINUCLEOTIDE × 4 PHB P-HYDROXYBENZOIC ACID × 4 PSL PYROSULFATE × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；310 K；ammonium sulfate, tris-sulfate, fad, edta, glutathion, sodium sulfite, p-hydroxybenzoate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 310K	Resolution 2.00 Å R-free 0.265

17 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	PHHY_PSEAE
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	1ius
Deposition date deposition_date	1995-11-22
Structure title title	P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE AT PH 5.0
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	22.64 Å
Radius of gyration Rg (electron density) rg_electron	21.58 Å
Forward intensity I(0) i0	35273500.00
Molecular weight molecular_weight	45226.0 kDa
Excluded volume excluded_volume	56402 Å³
Envelope volume envelope_volume	65882 Å³
Hydration-shell volume shell_volume	25130 Å³
Envelope diameter envelope_diameter	75.7 Å
Shell Rg shell_rg	28.70 Å
Envelope Rg envelope_rg	21.83 Å
Shape Rg shape_rg	21.58 Å
Total Rg total_rg	22.42 Å
Total atoms total_atoms	3187
Residues n_residues	394
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	72.9 Å
Rg (real space) rg_real	22.58 Å
Rg uncertainty (real space) rg_real_error	0.35 Å
I(0) (real space) i0_real	3.5270e+07
I(0) uncertainty (real space) i0_real_error	3.8900e+05
Rg (reciprocal space) rg_reciprocal	22.60 Å
I(0) (reciprocal space) i0_reciprocal	35270000.0000
Solution quality estimate total_estimate	0.8914
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.5 Å
Skewness Skewness skewness	0.312
Kurtosis Kurtosis kurtosis	-0.354
Angular range angular_range	— – 0.3500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	11990000.0000
Real-space data points n_real_points	67
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.866; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.987

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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	44382.5 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	3394

MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREACGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISRQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLSEKVEDWSDERFWTELKARLPSEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE

来源 Source

来源生物 organism	Pseudomonas aeruginosa
NCBI Class编号 ncbi_taxonomy_id	287

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	4-AMINOBENZOIC ACID
Molecular weight formula_weight	137.1 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	207

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1iusa1
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	d1iusa2
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	1iusA01
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	1iusA02
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 (4)

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Unit-cell length a length_a	71.710 Å
Unit-cell length b length_b	146.570 Å
Unit-cell length c length_c	88.390 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	2.200 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	0.1670
R_work r_work	0.1670
R_free r_free	—

fit	/app/data/saxs_computation/iu/1ius/1ius.fit
pddf	/app/data/pr_computation/iu/1ius/1ius.pr.out
profile	/app/data/saxs_computation/iu/1ius/1ius.dat

P-HYDROXYBENZOATE HYDROXYLASE COMPLEXED WITH 4-AMINOBENZOATE AT PH 5.0

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

P-HYDROXYBENZOATE HYDROXYLASE

State in the Current Structure

Other States of the Same Protein in the Database

SAXS scattering curve SAXS Profile

P(r) Distance Distribution P(r) Distribution

2. Structure Basics 2. Structure Basics

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

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

5. Crystallography and Experiment 5. Crystallography & Experiment

Unit cell Unit Cell

Symmetry Symmetry

Refinement Refinement

Diffraction experiment Diffraction