SAXSdb — 8v4a

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

Tryptophanase

Proteus vulgaris

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count	Chain A； UniProt 1–467 Chain B； UniProt 1–467 Chain C； UniProt 1–467 Chain D； UniProt 1–467	Not recorded	K POTASSIUM ION × 4 YAE (E)-S-ethyl-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-homocysteine × 2 YAR (2E)-4-(ethylsulfanyl)-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}butanoic acid × 2 DMS DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；295 K；0.1 M Potassium phosphate, pH 8.0, 0.1 mM PLP, 1 mM DTT, 0.2 M CsCl, 22% PEG 4000	Resolution 1.96 Å R-free 0.224

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 8V4A	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1AX4 TRYPTOPHANASE FROM PROTEUS VULGARIS Deposited 1997-10-28	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–467（467 aa） Chain B 1–467（467 aa） Chain C 1–467（467 aa） Chain D 1–467（467 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	K POTASSIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions pH 7.8；27 % PEG 4000, 0.1 M POTASSIUM PHOSPHATE BUFFER PH 7.8, 0.25 MM PYRIDOXAL 5'-PHOSPHATE, 5MM DTT, 0.1 M CSCL.	Resolution 2.10 Å R-free 0.227
5W19 Tryptophan indole-lyase complex with oxindolyl-L-alanine Deposited 2017-06-02	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–467（467 aa） Chain B 1–467（467 aa） Chain C 1–467（467 aa） Chain D 1–467（467 aa）	Not recorded	K POTASSIUM ION × 4 9TD 1-carboxy-1-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]azaniumyl}-2-[(3R)-2-oxo-2,3-dihydro-1H-indol-3-yl]ethan-1-ide × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；35 mM potassium phosphate, 0.05 M HEPES, 0.3 M KCl, 11% PEG 4000	Resolution 2.10 Å R-free 0.244
5W1B Tryptophan indole-lyase Deposited 2017-06-02	Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–467（467 aa） Chain B 1–467（467 aa） Chain C 1–467（467 aa） Chain D 1–467（467 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	K POTASSIUM ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7；293 K；35 mM potassium phosphate, 0.05 M HEPES, 0.3 M KCl, 11% PEG 4000	Resolution 2.00 Å R-free 0.252
8V2K Proteus vulgaris tryptophan indole-lyase complexed with L-alanine Deposited 2023-11-22	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–467（467 aa） Chain B 1–467（467 aa） Chain C 1–467（467 aa） Chain D 1–467（467 aa）	Not recorded	K POTASSIUM ION × 4 F0G (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-alanine × 2 DMS DIMETHYL SULFOXIDE × 2 PLI (2E)-2-{[(Z)-{3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4(1H)-YLIDENE}METHYL]IMINO}PROPANOIC ACID × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；295 K；0.1 M potassium phosphate, pH 8.0, 0.1 mM pyrodoxal-5'-phosphate, 1 mM DTT, 0.2 M CsCl, 22% PEG 4000	Resolution 1.81 Å R-free 0.231
8V6P Proteus vulgaris tryptophan indole-lyase complexed with 7-aza-L-tryptophan Deposited 2023-12-02	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–467（467 aa） Chain B 1–467（467 aa） Chain C 1–467（467 aa） Chain D 1–467（467 aa）	Not recorded	K POTASSIUM ION × 2 A1ACN (E)-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-3-(1H-pyrrolo[2,3-b]pyridin-3-yl)-L-alanine × 2 DMS DIMETHYL SULFOXIDE × 1 A1ABZ (2E)-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}-3-(1H-pyrrolo[2,3-b]pyridin-3-yl)propanoic acid × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8；295 K；0.1 M potassium phosphate, pH 8.0, 1 mM DTT, 0.1 mM PLP, 0.2 M CsCl, 22% PEG 4000	Resolution 1.74 Å R-free 0.228
8V9P Proteus vulgaris tryptophan indole-lyase complexed with (3S)-dioxindolyl-L-alanine Deposited 2023-12-08	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–467（467 aa） Chain B 1–467（467 aa） Chain C 1–467（467 aa） Chain D 1–467（467 aa）	Not recorded	K POTASSIUM ION × 4 YQK (2~{E})-2-[(~{Z})-[2-methyl-3-oxidanyl-5-[[oxidanyl-bis(oxidanylidene)-$l^{6}-phosphanyl]oxymethyl]-1~{H}-pyridin-4-ylidene]methyl]imino-3-[(3~{S})-3-oxidanyl-2-oxidanylidene-1~{H}-indol-3-yl]propanoic acid × 4 DMS DIMETHYL SULFOXIDE × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；295 K；0.1 M potassium phosphate, pH 8.0, 1 mM DTT, 0.1 mM PLP, 22% PEG 4000, 0.2 M CsCl	Resolution 1.85 Å R-free 0.247
9BLV Proteus vulgaris tryptophan indole-lyase complexed with L-Trp and benzimidazole Deposited 2024-05-01	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–467（467 aa） Chain B 1–467（467 aa） Chain C 1–467（467 aa） Chain D 1–467（467 aa）	Not recorded	K POTASSIUM ION × 4 BZI BENZIMIDAZOLE × 2 0JO 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid × 2 DMS DIMETHYL SULFOXIDE × 2 PLT [3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDIN-4-YLMETHYL]-L-TRYPTOPHANE × 1 A1A2Z N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-tryptophan × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M potassium phosphate, pH 8, 0.2 M CsCl, 22% PEG 4000	Resolution 1.78 Å R-free 0.247
9BNJ Proteus vulgaris tryptophan indole-lyase aminoacrylate complex with benzimidazole Deposited 2024-05-02	Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 1–467（467 aa） Chain B 1–467（467 aa） Chain C 1–467（467 aa） Chain D 1–467（467 aa）	Not recorded	K POTASSIUM ION × 4 BZI BENZIMIDAZOLE × 5 DMS DIMETHYL SULFOXIDE × 1 0JO 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid × 4 CL CHLORIDE ION × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M potassium phosphate, pH 8.0, 1 mM DTT, 0.1 mM PLP, 0.2 M KCl, 22% PEG 4000	Resolution 1.51 Å R-free 0.180
9DY7 Proteus vulgaris tryptophan indole-lyase complexed with L-ethionine and Na+ Deposited 2024-10-13	Different construct Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric	Chain A 2–467（466 aa） Chain B 2–467（466 aa） Chain C 2–467（466 aa） Chain D 2–467（466 aa）	Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF)	DMS DIMETHYL SULFOXIDE × 4 EDO 1,2-ETHANEDIOL × 2 ESC 2-AMINO-4-ETHYL SULFANYL BUTYRIC ACID × 2 NA SODIUM ION × 4 YAR (2E)-4-(ethylsulfanyl)-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}butanoic acid × 1 YAE (E)-S-ethyl-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-homocysteine × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；293 K；0.1 M potassium phosphate, pH 8.0, 1 mM DTT, 0.1 mM PLP, 0.2 M KCl, 22% PEG 4000	Resolution 1.87 Å R-free 0.185

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	TNAA_PROVU
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–467； UniProt 1–467 Author chain B； PDBConstruct 1–467； UniProt 1–467 Author chain C； PDBConstruct 1–467； UniProt 1–467 Author chain D； PDBConstruct 1–467； UniProt 1–467

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	8v4a
Deposition date deposition_date	2023-11-28
Structure title title	Proteus vulgaris tryptophan indole-lyase complexed with L-ethionine
Keywords keywords	;pyridoxal-5'-phosphate, fold I, tetramer, LYASE ;; LYASE
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	37.07 Å
Radius of gyration Rg (electron density) rg_electron	36.48 Å
Forward intensity I(0) i0	642279000.00
Molecular weight molecular_weight	211070.0 kDa
Excluded volume excluded_volume	265360 Å³
Envelope volume envelope_volume	308320 Å³
Hydration-shell volume shell_volume	65772 Å³
Envelope diameter envelope_diameter	116.2 Å
Shell Rg shell_rg	45.96 Å
Envelope Rg envelope_rg	36.80 Å
Shape Rg shape_rg	36.50 Å
Total Rg total_rg	36.92 Å
Total atoms total_atoms	14850
Residues n_residues	1863
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	116.7 Å
Rg (real space) rg_real	36.89 Å
Rg uncertainty (real space) rg_real_error	0.68 Å
I(0) (real space) i0_real	6.4230e+08
I(0) uncertainty (real space) i0_real_error	1.0180e+07
Rg (reciprocal space) rg_reciprocal	37.00 Å
I(0) (reciprocal space) i0_reciprocal	642300000.0000
Solution quality estimate total_estimate	0.8293
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	1
Primary peak position r_peak_primary	46.1 Å
Skewness Skewness skewness	0.181
Kurtosis Kurtosis kurtosis	-0.552
Angular range angular_range	— – 0.2150 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	505100000.0000
Real-space data points n_real_points	44
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.000

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (6)

Entity 1 Entity 1 polymer

Description description	Tryptophanase
Molecular weight formula_weight	52559.0 kDa
EC 编号 ec_number	4.1.99.1
Source method src_method	man
Copy count entity_count	4

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C,D
Atom count atom_count	16294

MAKRIVEPFRIKMVEKIRVPSREEREAALKEAGYNPFLLPSSAVYIDLLTDSGTNAMSDHQWAAMITGDEAYAGSRNYYDLKDKAKELFNYDYIIPAHQGRGAENILFPVLLKYKQKEGKAKNPVFISNFHFDTTAAHVELNGCKAINIVTEKAFDSETYDDWKGDFDIKKLKENIAQHGADNIVAIVSTVTCNSAGGQPVSMSNLKEVYEIAKQHGIFVVMDSARFCENAYFIKARDPKYKNATIKEVIFDMYKYADALTMSAKKDPLLNIGGLVAIRDNEEIFTLARQRCVPMEGFVTYGGLAGRDMAAMVQGLEEGTEEEYLHYRIGQVKYLGDRLREAGIPIQYPTGGHAVFVDCKKLVPQIPGDQFPAQAVINALYLESGVRAVEIGSFLLGRDPATGEQKHADMEFMRLTIARRVYTNDHMDYIADALIGLKEKFATLKGLEFEYEPPVLRHFTARLKPIE

来源 Source

来源生物 organism	Proteus vulgaris
NCBI Class编号 ncbi_taxonomy_id	585
宿主生物 host_organism	Escherichia coli BL21(DE3)

Entity 2 Entity 2 non-polymer

Description description	POTASSIUM ION
Molecular weight formula_weight	39.1 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 3 Entity 3 non-polymer

Description description	(E)-S-ethyl-N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene)-L-homocysteine
Molecular weight formula_weight	392.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 4 Entity 4 non-polymer

Description description	(2E)-4-(ethylsulfanyl)-2-{[(Z)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4(1H)-ylidene}methyl]imino}butanoic acid
Molecular weight formula_weight	392.4 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 5 Entity 5 non-polymer

Description description	DIMETHYL SULFOXIDE
Molecular weight formula_weight	78.1 kDa
Source method src_method	syn
Copy count entity_count	1

Entity 6 Entity 6 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1187

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8. Citations (1)

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Unit-cell length a length_a	150.750 Å
Unit-cell length b length_b	207.080 Å
Unit-cell length c length_c	60.830 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	16

Space group space_group	P 21 21 2
Space-group number int_tables_number	18
Crystal system crystal_system	orthorhombic

Resolution resolution	1.960 Å
Low-resolution limit resolution_low	62.760 Å
R factor r_factor	0.1779
R_work r_work	0.1768
R_free r_free	0.2241

fit	/app/data/saxs_computation/v4/8v4a/8v4a.fit
pddf	/app/data/pr_computation/v4/8v4a/8v4a.pr.out
profile	/app/data/saxs_computation/v4/8v4a/8v4a.dat

Proteus vulgaris tryptophan indole-lyase complexed with L-ethionine

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

Tryptophanase

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