SAXSdb — 1cc6

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

PROTEIN (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 monomer Monomer Protein × 1 PDB declaration: monomeric（1） Consistent with protein copy count	Chain A； UniProt 1–394	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

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 1CC6	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 oligomeric state Different ligand/ion Different experimental conditions	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 oligomeric state 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 oligomeric state 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 experimental conditions	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 oligomeric state Different ligand/ion Different experimental conditions	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 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 oligomeric state Different ligand/ion 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
1CJ2 MUTANT GLN34ARG OF PARA-HYDROXYBENZOATE HYDROXYLASE Deposited 1999-04-21	Different construct Different mutation/modification Different oligomeric state 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 oligomeric state 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 oligomeric state 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：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 oligomeric state 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：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 oligomeric state 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 oligomeric state 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
1PBB 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 mutation/modification Different oligomeric state 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 2.50 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 mutation/modification Different oligomeric state 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 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 mutation/modification Different oligomeric state 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 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 mutation/modification Different oligomeric state 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 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 mutation/modification Different oligomeric state 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 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 mutation/modification Different oligomeric state 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	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 mutation/modification Different oligomeric state 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 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 mutation/modification Different oligomeric state 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	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	1cc6
Deposition date deposition_date	1999-03-04
Structure title title	PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY.
Keywords keywords	OXIDOREDUCTASE, HYDROXYBENZOATE; 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	22.61 Å
Radius of gyration Rg (electron density) rg_electron	21.57 Å
Forward intensity I(0) i0	34464700.00
Molecular weight molecular_weight	44770.0 kDa
Excluded volume excluded_volume	55870 Å³
Envelope volume envelope_volume	65192 Å³
Hydration-shell volume shell_volume	24940 Å³
Envelope diameter envelope_diameter	74.4 Å
Shell Rg shell_rg	28.60 Å
Envelope Rg envelope_rg	21.80 Å
Shape Rg shape_rg	21.57 Å
Total Rg total_rg	22.40 Å
Total atoms total_atoms	3156
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	72.3 Å
Rg (real space) rg_real	22.56 Å
Rg uncertainty (real space) rg_real_error	0.41 Å
I(0) (real space) i0_real	3.4460e+07
I(0) uncertainty (real space) i0_real_error	4.7400e+05
Rg (reciprocal space) rg_reciprocal	22.57 Å
I(0) (reciprocal space) i0_reciprocal	34460000.0000
Solution quality estimate total_estimate	0.8938
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	26.3 Å
Skewness Skewness skewness	0.313
Kurtosis Kurtosis kurtosis	-0.362
Angular range angular_range	— – 0.3500 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	11640000.0000
Real-space data points n_real_points	67
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.876; 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	PROTEIN (P-HYDROXYBENZOATE HYDROXYLASE)
Molecular weight formula_weight	44294.4 kDa
EC 编号 ec_number	1.14.13.2
Mutation mutation	R166S, C116S
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	3374

MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQTPDYVLGRIRAGVLEQGMVDLLREAGVDRRMARDGLVHEGVEIAFAGQRRRIDLKRLSGGKTVTVYGQTEVTRDLMEAREASGATTVYQAAEVRLHDLQGERPYVTFERDGERLRLDCDYIAGCDGFHGISSQSIPAERLKVFERVYPFGWLGLLADTPPVSHELIYANHPRGFALCSQRSATRSRYYVQVPLTEKVEDWSDERFWTELKARLPAEVAEKLVTGPSLEKSIAPLRSFVVEPMQHGRLFLAGDAAHIVPPTGAKGLNLAASDVSTLYRLLLKAYREGRGELLERYSAICLRRIWKAERFSWWMTSVLHRFPDTDAFSQRIQQTELEYYLGSEAGLATIAENYVGLPYEEIE

来源 Source

来源生物 organism	Pseudomonas fluorescens
NCBI Class编号 ncbi_taxonomy_id	294
宿主生物 host_organism	Escherichia coli

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	P-HYDROXYBENZOIC ACID
Molecular weight formula_weight	138.1 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	218

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7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1cc6a1
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	d1cc6a2
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	1cc6A01
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	1cc6A02
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 (10)

Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability.

Febs Lett. (1999)

PMID: 10025942 · DOI: 10.1016/S0014-5793(98)01726-8 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)

PMID: 7756982 · DOI: 10.1002/pro.5560031210

;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

Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3 A resolution.

Proteins (1992)

PMID: 1409567 · DOI: 10.1002/prot.340140205

Engineering of microheterogeneity-resistant p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.

Febs Lett. (1990)

PMID: 2269354 · DOI: 10.1016/0014-5793(90)80843-8

;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)

PMID: 2553983 · DOI: 10.1016/0022-2836(89)90158-7

;The coenzyme analogue adenosine 5-diphosphoribose displaces FAD in the active site of p-hydroxybenzoate hydroxylase. An x-ray crystallographic investigation. ;

Biochemistry (1989)

PMID: 2819062 · DOI: 10.1021/bi00444a011

Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate.

J.Mol.Biol. (1988)

PMID: 3351945 · DOI: 10.1016/0022-2836(88)90307-5

Crystal structure of p-hydroxybenzoate hydroxylase.

J.Mol.Biol. (1979)

PMID: 40036 · DOI: 10.1016/0022-2836(79)90301-2

Crystallization and preliminary x-ray investigation of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens.

J.Biol.Chem. (1975)

PMID: 807574

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Unit-cell length a length_a	72.200 Å
Unit-cell length b length_b	146.800 Å
Unit-cell length c length_c	88.900 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	8.000 Å
R factor r_factor	—
R_work r_work	0.1850
R_free r_free	—

fit	/app/data/saxs_computation/cc/1cc6/1cc6.fit
pddf	/app/data/pr_computation/cc/1cc6/1cc6.pr.out
profile	/app/data/saxs_computation/cc/1cc6/1cc6.dat

PHE161 AND ARG166 VARIANTS OF P-HYDROXYBENZOATE HYDROXYLASE. IMPLICATIONS FOR NADPH RECOGNITION AND STRUCTURAL STABILITY.

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

PROTEIN (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