1hrp

CRYSTAL STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN

Method: X-RAY DIFFRACTION Dmax: 84.2 Å Quality: REASONABLE

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

HUMAN CHORIONIC GONADOTROPIN

Homo sapiens

UniProt P01215

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 25–116 Not recorded HUMAN CHORIONIC GONADOTROPIN × 1 (P01233) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å R-free 0.314
2 Other combination Heteromer Protein × 4 其他Polymer 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 25–116 Not recorded HUMAN CHORIONIC GONADOTROPIN × 2 (P01233) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å R-free 0.314

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.

15 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLHA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–92; UniProt 25–116

HUMAN CHORIONIC GONADOTROPIN

OrganismNot specified

UniProt P01233

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 21–165 Not recorded HUMAN CHORIONIC GONADOTROPIN × 1 (P01215) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å R-free 0.314
2 Other combination Heteromer Protein × 4 其他Polymer 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 21–165 Not recorded HUMAN CHORIONIC GONADOTROPIN × 2 (P01215) 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 3.00 Å R-free 0.314

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 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CGHB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–145; UniProt 21–165

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 1hrp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1hrp
Deposition date deposition_date1994-08-15
Structure title titleCRYSTAL STRUCTURE OF HUMAN CHORIONIC GONADOTROPIN
Keywords keywordsHORMONE; HORMONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.00
Radius of gyration Rg (electron density) rg_electron21.14
Forward intensity I(0) i010228400.00
Molecular weight molecular_weight22435.0 kDa
Excluded volume excluded_volume27596 ų
Envelope volume envelope_volume34496 ų
Hydration-shell volume shell_volume15332 ų
Envelope diameter envelope_diameter84.7
Shell Rg shell_rg25.55
Envelope Rg envelope_rg21.50
Shape Rg shape_rg21.19
Total Rg total_rg21.66
Total atoms total_atoms1550
Residues n_residues196
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 dmax84.2
Rg (real space) rg_real21.32
Rg uncertainty (real space) rg_real_error0.97
I(0) (real space) i0_real1.0230e+07
I(0) uncertainty (real space) i0_real_error1.6010e+05
Rg (reciprocal space) rg_reciprocal21.26
I(0) (reciprocal space) i0_reciprocal10230000.0000
Solution quality estimate total_estimate0.7255
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary19.5
Skewness Skewness skewness0.730
Kurtosis Kurtosis kurtosis0.285
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1771000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.396; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.280; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1hrpa_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.4 — Gonadodropin/Follitropin
Domain ID domain_idd1hrpb_
Class classg — Small proteins
Fold Fold foldg.17 — Cystine-knot cytokines
Superfamily Superfamily superfamilyg.17.1 — Cystine-knot cytokines
Family Family familyg.17.1.4 — Gonadodropin/Follitropin

CATH v4.4 (2 domains)

Domain ID domain_id1hrpA00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines
Domain ID domain_id1hrpB00
Class class2 — Mainly Beta
Architecture architecture10 — Ribbon
Topology topology90 — Cystine Knot Cytokines, subunit B
Homologous superfamily homologous superfamily10 — Cystine-knot cytokines

8. Citations (2)

9. Files and Curves (10)