SAXSdb — 1a3g

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

BRANCHED-CHAIN AMINO ACID 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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count	Chain A； UniProt 1–308 Chain B； UniProt 1–308 Chain C； UniProt 1–308	Not recorded	PLP PYRIDOXAL-5'-PHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions：pH 7.5；PROTEIN WAS CRYSTALLIZED FROM 28% PEG 400, 200MM MGCL2, 100MM HEPES, PH 7.5	Resolution 2.50 Å R-free 0.258

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 1A3G	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1I1K CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE. Deposited 2001-02-02	Different construct Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–309（309 aa） Chain B 1–309（309 aa） Chain C 1–309（309 aa）	Not recorded	PLP PYRIDOXAL-5'-PHOSPHATE × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG400, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.10 Å R-free 0.231
1I1M CRYSTAL STRUCTURE OF ESCHERICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE. Deposited 2001-02-02	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–309（309 aa） Chain B 1–309（309 aa） Chain C 1–309（309 aa）	Not recorded	PLP PYRIDOXAL-5'-PHOSPHATE × 6 4MV 4-METHYL VALERIC ACID × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG400, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.40 Å R-free 0.215
1I1M CRYSTAL STRUCTURE OF ESCHERICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE. Deposited 2001-02-02	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 1–309（309 aa） Chain B 1–309（309 aa） Chain C 1–309（309 aa）	Not recorded	PLP PYRIDOXAL-5'-PHOSPHATE × 6 4MV 4-METHYL VALERIC ACID × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG400, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.40 Å R-free 0.215
1IYD CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE Deposited 2002-08-07	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 0–308（309 aa） Chain B 0–308（309 aa） Chain C 0–308（309 aa）	Not recorded	PLP PYRIDOXAL-5'-PHOSPHATE × 6 GUA GLUTARIC ACID × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG400, HEPES, MgCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 2.15 Å R-free 0.242
1IYE CRYSTAL STRUCTURE OF ESCHELICHIA COLI BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE Deposited 2002-08-07	Different construct Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 6 PDB declaration: hexameric	Chain A 0–308（309 aa） Chain B 0–308（309 aa） Chain C 0–308（309 aa）	Not recorded	PGU N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid × 6	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；293 K；PEG400, HEPES, MgCl2, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K	Resolution 1.82 Å R-free 0.239

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence

UniProt name	ILVE_ECOLI
Isoform	—
PDB entities	1
Chains and sequence ranges	Author chain A； PDBConstruct 1–308； UniProt 1–308 Author chain B； PDBConstruct 1–308； UniProt 1–308 Author chain C； PDBConstruct 1–308； UniProt 1–308

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	1a3g
Deposition date deposition_date	1998-01-21
Structure title title	BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI
Keywords keywords	AMINOTRANSFERASE, PYRIDOXAL ENZYME; AMINOTRANSFERASE
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	32.27 Å
Radius of gyration Rg (electron density) rg_electron	31.40 Å
Forward intensity I(0) i0	155682000.00
Molecular weight molecular_weight	98644.0 kDa
Excluded volume excluded_volume	122980 Å³
Envelope volume envelope_volume	155060 Å³
Hydration-shell volume shell_volume	41288 Å³
Envelope diameter envelope_diameter	100.9 Å
Shell Rg shell_rg	38.33 Å
Envelope Rg envelope_rg	31.28 Å
Shape Rg shape_rg	31.40 Å
Total Rg total_rg	31.97 Å
Total atoms total_atoms	6954
Residues n_residues	885
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	100.0 Å
Rg (real space) rg_real	32.17 Å
Rg uncertainty (real space) rg_real_error	0.55 Å
I(0) (real space) i0_real	1.5570e+08
I(0) uncertainty (real space) i0_real_error	2.2770e+06
Rg (reciprocal space) rg_reciprocal	32.22 Å
I(0) (reciprocal space) i0_reciprocal	155700000.0000
Solution quality estimate total_estimate	0.9085
Solution quality rating solution_quality	EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	36.7 Å
Skewness Skewness skewness	0.206
Kurtosis Kurtosis kurtosis	-0.613
Angular range angular_range	— – 0.2450 Å⁻¹
Current regularization parameter α current_alpha	0.0001
Highest regularization parameter α highest_alpha	16610000.0000
Real-space data points n_real_points	50
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.957; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.934

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE
Molecular weight formula_weight	34000.4 kDa
EC 编号 ec_number	2.6.1.42
Source method src_method	nat
Copy count entity_count	3

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,B,C
Atom count atom_count	7474

TTKKADYIWFNGEMVRWEDAKVHVMSHALHYGTSVFEGIRCYDSHKGPVVFRHREHMQRLHDSAKIYRFPVSQSIDELMEACRDVIRKNNLTSAYIRPLIFVGDVGMGVNPPAGYSTDVIIAAFPWGAYLGAEALEQGIDAMVSSWNRAAPNTIPTAAKAGGNYLSSLLVGSEARRHGYQEGIALDVNGYISEGAGENLFEVKDGVLFTPPFTSSALPGITRDAIIKLAKELGIEVREQVLSRESLYLADEVFMSGTAAEITPVRSVDGIQVGEGRCGPVTKRIQQAFFGLFTGETEDKWGWLDQVNQ

Entity 2 Entity 2 non-polymer

Description description	PYRIDOXAL-5'-PHOSPHATE
Molecular weight formula_weight	247.1 kDa
Source method src_method	syn
Copy count entity_count	3

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	520

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7. Fold Classification (SCOP + CATH) 9 domains

SCOP 2.08 (3 domains)

Domain ID domain_id	d1a3ga_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.17 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Superfamily Superfamily superfamily	e.17.1 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Family Family family	e.17.1.1 — D-aminoacid aminotransferase-like PLP-dependent enzymes

Domain ID domain_id	d1a3gb_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.17 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Superfamily Superfamily superfamily	e.17.1 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Family Family family	e.17.1.1 — D-aminoacid aminotransferase-like PLP-dependent enzymes

Domain ID domain_id	d1a3gc_
Class class	e — Multi-domain proteins (alpha and beta)
Fold Fold fold	e.17 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Superfamily Superfamily superfamily	e.17.1 — D-aminoacid aminotransferase-like PLP-dependent enzymes
Family Family family	e.17.1.1 — D-aminoacid aminotransferase-like PLP-dependent enzymes

CATH v4.4 (6 domains)

Domain ID domain_id	1a3gA01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aminotransferase class 4, branched-chain amino acid transferase, N-terminal domain

Domain ID domain_id	1a3gA02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	10 — D-amino Acid Aminotransferase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — D-amino Acid Aminotransferase, subunit A, domain 2

Domain ID domain_id	1a3gB01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aminotransferase class 4, branched-chain amino acid transferase, N-terminal domain

Domain ID domain_id	1a3gB02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	10 — D-amino Acid Aminotransferase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — D-amino Acid Aminotransferase, subunit A, domain 2

Domain ID domain_id	1a3gC01
Class class	3 — Alpha Beta
Architecture architecture	30 — 2-Layer Sandwich
Topology topology	470 — D-amino Acid Aminotransferase; Chain A, domain 1
Homologous superfamily homologous superfamily	10 — Aminotransferase class 4, branched-chain amino acid transferase, N-terminal domain

Domain ID domain_id	1a3gC02
Class class	3 — Alpha Beta
Architecture architecture	20 — Alpha-Beta Barrel
Topology topology	10 — D-amino Acid Aminotransferase; Chain A, domain 2
Homologous superfamily homologous superfamily	10 — D-amino Acid Aminotransferase, subunit A, domain 2

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8. Citations (1)

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Unit-cell length a length_a	135.100 Å
Unit-cell length b length_b	144.000 Å
Unit-cell length c length_c	102.900 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	136.10 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	12

Space group space_group	C 1 2 1
Space-group number int_tables_number	5
Crystal system crystal_system	—

Resolution resolution	2.500 Å
Low-resolution limit resolution_low	10.000 Å
R factor r_factor	0.1880
R_work r_work	0.1880
R_free r_free	0.2580

fit	/app/data/saxs_computation/a3/1a3g/1a3g.fit
pddf	/app/data/pr_computation/a3/1a3g/1a3g.pr.out
profile	/app/data/saxs_computation/a3/1a3g/1a3g.dat

BRANCHED-CHAIN AMINO ACID AMINOTRANSFERASE FROM ESCHERICHIA COLI

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

BRANCHED-CHAIN AMINO ACID 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