SAXSdb — 1bw0

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

PROTEIN (TYROSINE AMINOTRANSFERASE)

OrganismNot specified

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 1–416 Chain B； UniProt 1–416	Non-standard monomer：Yes (specific site not provided by mmCIF)	No other associated polymer	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7；DIALYSIS OF 2.6 MG/ML PROTEIN AGAINST 25 % (W/W) PEG 8000, 5 MM PLP, 0.1 M PHOSPHATE/CITRATE, PH 7.0, 285 K	Resolution 2.50 Å R-free 0.214

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence

UniProt name	ATTY_TRYCR
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–416； UniProt 1–416 Author chain B； PDBConstruct 1–416； UniProt 1–416

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	1bw0
Deposition date deposition_date	1998-09-28
Structure title title	CRYSTAL STRUCTURE OF TYROSINE AMINOTRANSFERASE FROM TRYPANOSOMA CRUZI
Keywords keywords	;TYROSINE CATABOLISM, TRANSFERASE, AMINOTRANSFERASE, PYRIDOXAL-5'-PHOSPHATE, PLP ;; TRANSFERASE
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	29.38 Å
Radius of gyration Rg (electron density) rg_electron	28.39 Å
Forward intensity I(0) i0	133001000.00
Molecular weight molecular_weight	92050.0 kDa
Excluded volume excluded_volume	115510 Å³
Envelope volume envelope_volume	136260 Å³
Hydration-shell volume shell_volume	39441 Å³
Envelope diameter envelope_diameter	108.1 Å
Shell Rg shell_rg	36.39 Å
Envelope Rg envelope_rg	28.53 Å
Shape Rg shape_rg	28.40 Å
Total Rg total_rg	29.08 Å
Total atoms total_atoms	6472
Residues n_residues	823
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	99.9 Å
Rg (real space) rg_real	29.34 Å
Rg uncertainty (real space) rg_real_error	0.75 Å
I(0) (real space) i0_real	1.3300e+08
I(0) uncertainty (real space) i0_real_error	1.9970e+06
Rg (reciprocal space) rg_reciprocal	29.36 Å
I(0) (reciprocal space) i0_reciprocal	133000000.0000
Solution quality estimate total_estimate	0.8679
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	35.1 Å
Skewness Skewness skewness	0.345
Kurtosis Kurtosis kurtosis	-0.270
Angular range angular_range	— – 0.2700 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	49500000.0000
Real-space data points n_real_points	55
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.810; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.851

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_id	d1bw0a_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.67 — PLP-dependent transferase-like
Superfamily Superfamily superfamily	c.67.1 — PLP-dependent transferases
Family Family family	c.67.1.1 — AAT-like

Domain ID domain_id	d1bw0b_
Class class	c — Alpha and beta proteins (a/b)
Fold Fold fold	c.67 — PLP-dependent transferase-like
Superfamily Superfamily superfamily	c.67.1 — PLP-dependent transferases
Family Family family	c.67.1.1 — AAT-like

CATH v4.4 (4 domains)

Domain ID domain_id	1bw0A01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily	10 — Aspartate Aminotransferase, domain 1

Domain ID domain_id	1bw0A02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	640 — Aspartate Aminotransferase; domain 2
Homologous superfamily homologous superfamily	10 — Type I PLP-dependent aspartate aminotransferase-like (Major domain)

Domain ID domain_id	1bw0B01
Class class	3 — Alpha Beta
Architecture architecture	90 — Alpha-Beta Complex
Topology topology	1150 — Aspartate Aminotransferase, domain 1
Homologous superfamily homologous superfamily	10 — Aspartate Aminotransferase, domain 1

Domain ID domain_id	1bw0B02
Class class	3 — Alpha Beta
Architecture architecture	40 — 3-Layer(aba) Sandwich
Topology topology	640 — Aspartate Aminotransferase; domain 2
Homologous superfamily homologous superfamily	10 — Type I PLP-dependent aspartate aminotransferase-like (Major domain)

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8. Citations (4)

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Unit-cell length a length_a	61.600 Å
Unit-cell length b length_b	102.200 Å
Unit-cell length c length_c	77.900 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	110.30 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	—
R_work r_work	0.1570
R_free r_free	0.2140

Description description	PROTEIN (TYROSINE AMINOTRANSFERASE)
Molecular weight formula_weight	46450.0 kDa
EC 编号 ec_number	2.6.1.5
Source method src_method	nat
Copy count entity_count	2

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B
Atom count atom_count	6590

CRYSTAL STRUCTURE OF TYROSINE AMINOTRANSFERASE FROM TRYPANOSOMA CRUZI

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

PROTEIN (TYROSINE AMINOTRANSFERASE)

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

6. Entities and Polymers Entities & Polymers (2)

Entity 1 Entity 1 polymer

Polymer Polymer

Entity 2 Entity 2 water

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

CATH v4.4 (4 domains)

8. Citations (4)

9. Files and Curves (10)

Files (7)

Curves (3)

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	118

fit	/app/data/saxs_computation/bw/1bw0/1bw0.fit
pddf	/app/data/pr_computation/bw/1bw0/1bw0.pr.out
profile	/app/data/saxs_computation/bw/1bw0/1bw0.dat