1ht8

THE 2.7 ANGSTROM RESOLUTION MODEL OF OVINE COX-1 COMPLEXED WITH ALCLOFENAC

Method: X-RAY DIFFRACTION Dmax: 100.7 Å Quality: EXCELLENT

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

PROSTAGLANDIN H2 SYNTHASE-1

OrganismNot specified

UniProt P05979

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 32–582 Chain B; UniProt 32–582 Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 BOG octyl beta-D-glucopyranoside × 3 HEM PROTOPORPHYRIN IX CONTAINING FE × 2 34C (3-CHLORO-4-PROPOXY-PHENYL)-ACETIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;291 K;PEG-4000, SODIUM CHLORIDE, BETA-OCTYL GLUCOSIDE, POTASSIUM PHOSPHATE (DIBASIC), pH 6.7, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.69 Å R-free 0.242

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.

20 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PGH1_SHEEP
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–551; UniProt 32–582 Author chain B; PDBConstruct 1–551; UniProt 32–582

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 1ht8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ht8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ht8
Deposition date deposition_date2000-12-29
Structure title titleTHE 2.7 ANGSTROM RESOLUTION MODEL OF OVINE COX-1 COMPLEXED WITH ALCLOFENAC
Keywords keywordsMEMBRANE PROTEIN, PEROXIDASE, DIOXYGENASE, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.23
Radius of gyration Rg (electron density) rg_electron31.34
Forward intensity I(0) i0247889000.00
Molecular weight molecular_weight131050.0 kDa
Excluded volume excluded_volume165650 ų
Envelope volume envelope_volume194890 ų
Hydration-shell volume shell_volume49855 ų
Envelope diameter envelope_diameter104.2
Shell Rg shell_rg40.16
Envelope Rg envelope_rg31.24
Shape Rg shape_rg31.32
Total Rg total_rg32.09
Total atoms total_atoms9242
Residues n_residues1102
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 dmax100.7
Rg (real space) rg_real32.08
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real2.4790e+08
I(0) uncertainty (real space) i0_real_error3.8880e+06
Rg (reciprocal space) rg_reciprocal32.15
I(0) (reciprocal space) i0_reciprocal247900000.0000
Solution quality estimate total_estimate0.9005
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.0
Skewness Skewness skewness0.213
Kurtosis Kurtosis kurtosis-0.489
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha80480000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.928; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1ht8a1
Class classa — All alpha proteins
Fold Fold folda.93 — Heme-dependent peroxidases
Superfamily Superfamily superfamilya.93.1 — Heme-dependent peroxidases
Family Family familya.93.1.2 — Myeloperoxidase-like
Domain ID domain_idd1ht8a2
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.1 — EGF-type module
Domain ID domain_idd1ht8b1
Class classa — All alpha proteins
Fold Fold folda.93 — Heme-dependent peroxidases
Superfamily Superfamily superfamilya.93.1 — Heme-dependent peroxidases
Family Family familya.93.1.2 — Myeloperoxidase-like
Domain ID domain_idd1ht8b2
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.11 — EGF/Laminin
Family Family familyg.3.11.1 — EGF-type module

CATH v4.4 (4 domains)

Domain ID domain_id1ht8A01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin
Domain ID domain_id1ht8A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology640 — Myeloperoxidase, subunit C
Homologous superfamily homologous superfamily10 — Haem peroxidase domain superfamily, animal type
Domain ID domain_id1ht8B01
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology25 — Laminin
Homologous superfamily homologous superfamily10 — Laminin
Domain ID domain_id1ht8B02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology640 — Myeloperoxidase, subunit C
Homologous superfamily homologous superfamily10 — Haem peroxidase domain superfamily, animal type

8. Citations (1)

9. Files and Curves (10)