Structure of human chorionic gonadotropin at 2.6 Å resolution from mad analysis of the selenomethionyl protein. Determined by X-ray diffraction at 2.6 Å resolution. Released 30 Sept 1994.
Explore 1HCN in 3D Show helices and sheets RCSB PDB PDBe
1HCN contains 4 α-helices and 20 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 6 | 1 | 1 |
| α-helix | 8 | 1 | |
| β-strand | 9 | 1 | 2 |
| β-strand | 11-14 | 4 | 3 |
| β-strand | 20 | 1 | 4 |
| β-strand | 23 | 1 | 4 |
| β-strand | 26-29 | 4 | 3 |
| β-strand | 30-38 | 9 | 2 |
| α-helix | 39-40 | 2 | |
| α-helix | 41-44 | 4 | |
| β-strand | 53-56 | 4 | 2 |
| β-strand | 59-69 | 11 | 5 |
| β-strand | 75-85 | 11 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7 | 1 | 1 |
| β-strand | 8 | 1 | 2 |
| β-strand | 10-18 | 9 | 2 |
| β-strand | 21 | 1 | 6 |
| β-strand | 23 | 1 | 6 |
| β-strand | 27-40 | 14 | 2 |
| β-strand | 45 | 1 | 5 |
| α-helix | 53-54 | 2 | |
| β-strand | 55-68 | 14 | 7 |
| β-strand | 79-92 | 14 | 7 |
| β-strand | 98-101 | 4 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Human chorionic gonadotropin | A | protein | 92 | Homo sapiens | P01215 (AlphaFold model) |
| Human chorionic gonadotropin | B | protein | 145 | P0DN86 (AlphaFold model) |
>1HCN_1 HUMAN CHORIONIC GONADOTROPIN (chains A) APDVQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCC VAKSYNRVTVMGGFKVENHTACHCSTCYYHKS
>1HCN_2 HUMAN CHORIONIC GONADOTROPIN (chains B) SKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYR DVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSS SKAPPPSLPSPSRLPGPSDTPILPQ
| ID | Name | Formula | Copies |
|---|---|---|---|
| NAG | 2-acetamido-2-deoxy-beta-D-glucopyranose | C8 H15 N O6 | 2 |
Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein. Wu, H., Lustbader, J.W., Liu, Y. et al. Structure (1994) 2:545-558. DOI 10.1016/S0969-2126(00)00054-X · PubMed
Other PDB entries of the same protein (UniProt P01215 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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