1bhs

HUMAN ESTROGENIC 17BETA-HYDROXYSTEROID DEHYDROGENASE

Method: X-RAY DIFFRACTION Dmax: 65.0 Å Quality: REASONABLE

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

17BETA-HYDROXYSTEROID DEHYDROGENASE

OrganismNot specified

UniProt P14061

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 1–327 Not recorded No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.20 Å R-free 0.229

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.

27 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name DHB1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–327; UniProt 1–327

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 1bhs

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bhs
Deposition date deposition_date1995-04-19
Structure title titleHUMAN ESTROGENIC 17BETA-HYDROXYSTEROID DEHYDROGENASE
Keywords keywordsSHORT-CHAIN DEHYDROGENASE, STEROID DEHYDROGENASE, ESTROGEN, HUMAN TYPE I 17BETA-HSD, HUMAN PLACENTAL 17BETA-HSD, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.86
Radius of gyration Rg (electron density) rg_electron19.71
Forward intensity I(0) i016586100.00
Molecular weight molecular_weight30979.0 kDa
Excluded volume excluded_volume39005 ų
Envelope volume envelope_volume46774 ų
Hydration-shell volume shell_volume20163 ų
Envelope diameter envelope_diameter66.8
Shell Rg shell_rg25.84
Envelope Rg envelope_rg19.75
Shape Rg shape_rg19.75
Total Rg total_rg20.49
Total atoms total_atoms2177
Residues n_residues284
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 dmax65.0
Rg (real space) rg_real20.79
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real1.6590e+07
I(0) uncertainty (real space) i0_real_error2.1090e+05
Rg (reciprocal space) rg_reciprocal20.81
I(0) (reciprocal space) i0_reciprocal16590000.0000
Solution quality estimate total_estimate0.7108
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.4
Skewness Skewness skewness0.259
Kurtosis Kurtosis kurtosis-0.388
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2691000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.909; Stabil: 1.000; Sysdev: 0.177; Positv: 1.000; Valcen: 0.998; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bhsa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamilyc.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family familyc.2.1.2 — Tyrosine-dependent oxidoreductases

CATH v4.4 (1 domains)

Domain ID domain_id1bhsA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain

8. Citations (2)

9. Files and Curves (10)