7q06

Crystal structure of TPADO in complex with 2-OH-TPA

Method: X-RAY DIFFRACTION Dmax: 124.9 Å Quality: GOOD

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

Terephthalate 1,2-dioxygenase, terminal oxygenase component subunit beta 1

Comamonas sp.

UniProt Q3C1E2

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–154 Chain B; UniProt 1–154 Chain C; UniProt 1–154 Not recorded Terephthalate 1,2-dioxygenase, terminal oxygenase component subunit alpha 2 × 3 (Q3C1D5) Lysozyme × 1 (P00698) SO4 SULFATE ION × 6 FES FE2/S2 (INORGANIC) CLUSTER × 3 FE FE (III) ION × 2 8IB 2-Hydroxyterephthalic acid × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;12.5% MPD, 12.5% PEG 3350, 12.5% PEG 1000, 0.3 M sodium nitrate, 0.3 M sodium phosphate dibasic, 0.3 M ammonium sulfate, 0.1 M buffer Imidazole/MES pH 6.5 Resolution 1.95 Å R-free 0.202

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TPDB1_COMSP
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–154; UniProt 1–154 Author chain B; PDBConstruct 1–154; UniProt 1–154 Author chain C; PDBConstruct 1–154; UniProt 1–154

Terephthalate 1,2-dioxygenase, terminal oxygenase component subunit alpha 2

Comamonas sp.

UniProt Q3C1D5

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain D; UniProt 1–413 Chain E; UniProt 1–413 Chain F; UniProt 1–413 Not recorded Terephthalate 1,2-dioxygenase, terminal oxygenase component subunit beta 1 × 3 (Q3C1E2) Lysozyme × 1 (P00698) SO4 SULFATE ION × 6 FES FE2/S2 (INORGANIC) CLUSTER × 3 FE FE (III) ION × 2 8IB 2-Hydroxyterephthalic acid × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;12.5% MPD, 12.5% PEG 3350, 12.5% PEG 1000, 0.3 M sodium nitrate, 0.3 M sodium phosphate dibasic, 0.3 M ammonium sulfate, 0.1 M buffer Imidazole/MES pH 6.5 Resolution 1.95 Å R-free 0.202

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TPDA2_COMSP
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 3–415; UniProt 1–413 Author chain E; PDBConstruct 3–415; UniProt 1–413 Author chain F; PDBConstruct 3–415; UniProt 1–413

Lysozyme

OrganismNot specified

UniProt P00698

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 heterocomplex Heteromer Protein × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain H; UniProt 19–147 Not recorded Terephthalate 1,2-dioxygenase, terminal oxygenase component subunit beta 1 × 3 (Q3C1E2) Terephthalate 1,2-dioxygenase, terminal oxygenase component subunit alpha 2 × 3 (Q3C1D5) SO4 SULFATE ION × 6 FES FE2/S2 (INORGANIC) CLUSTER × 3 FE FE (III) ION × 2 8IB 2-Hydroxyterephthalic acid × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;12.5% MPD, 12.5% PEG 3350, 12.5% PEG 1000, 0.3 M sodium nitrate, 0.3 M sodium phosphate dibasic, 0.3 M ammonium sulfate, 0.1 M buffer Imidazole/MES pH 6.5 Resolution 1.95 Å R-free 0.202

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.

1320 other PDB entries and 1450 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LYSC_CHICK
Isoform
PDB entities 3
Chains and sequence ranges Author chain H; PDBConstruct 1–129; UniProt 19–147

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.

SAXS scattering curve SAXS Profile

SAXS profile for 7q06

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7q06
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7q06
Deposition date deposition_date2021-10-14
Structure title titleCrystal structure of TPADO in complex with 2-OH-TPA
Keywords keywordsterephthalic acid, TPA, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier37.00
Radius of gyration Rg (electron density) rg_electron35.89
Forward intensity I(0) i0634873000.00
Molecular weight molecular_weight198580.0 kDa
Excluded volume excluded_volume245410 ų
Envelope volume envelope_volume307960 ų
Hydration-shell volume shell_volume67856 ų
Envelope diameter envelope_diameter135.8
Shell Rg shell_rg44.82
Envelope Rg envelope_rg35.84
Shape Rg shape_rg35.88
Total Rg total_rg36.44
Total atoms total_atoms27384
Residues n_residues1764
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

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

Maximum dimension Dmax dmax124.9
Rg (real space) rg_real36.75
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real6.3490e+08
I(0) uncertainty (real space) i0_real_error1.1140e+07
Rg (reciprocal space) rg_reciprocal36.91
I(0) (reciprocal space) i0_reciprocal635000000.0000
Solution quality estimate total_estimate0.7937
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.4
Skewness Skewness skewness0.115
Kurtosis Kurtosis kurtosis-0.420
Angular range angular_range— – 0.2150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha150800000.0000
Real-space data points n_real_points44
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.772; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 3 domains

CATH v4.4 (3 domains)

Domain ID domain_id7q06D01
Class class2 — Mainly Beta
Architecture architecture102 — 3-layer Sandwich
Topology topology10 — Rieske Iron-sulfur Protein
Homologous superfamily homologous superfamily10 — Rieske [2Fe-2S] iron-sulphur domain
Domain ID domain_id7q06E01
Class class2 — Mainly Beta
Architecture architecture102 — 3-layer Sandwich
Topology topology10 — Rieske Iron-sulfur Protein
Homologous superfamily homologous superfamily10 — Rieske [2Fe-2S] iron-sulphur domain
Domain ID domain_id7q06H01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology530 — Lysozyme
Homologous superfamily homologous superfamily10

8. Citations (1)

9. Files and Curves (10)