1HRP: Human chorionic gonadotropin

Crystal structure of human chorionic gonadotropin. Determined by X-ray diffraction at 3.0 Å resolution. Released 1 Nov 1994.

Method
X-ray diffraction
Resolution
3.0 Å
Organism
Homo sapiens
Chains
2
Atoms
1,550
Mol. weight
27.06 kDa
Ligands
NAG
Released
1 Nov 1994

Explore 1HRP in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1HRP contains 5 α-helices and 25 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.

Chain A: 2 helices, 11 β-strands

ElementResiduesLengthSheet
β-strand611
β-strand11-20102
β-strand23-38162
α-helix39-402
α-helix41-444
β-strand53-5752
β-strand58-6253
β-strand65-6734
β-strand7015
β-strand7415
β-strand7616
β-strand77-7934
β-strand82-8653
Chain B: 3 helices, 14 β-strands
ElementResiduesLengthSheet
β-strand711
β-strand812
β-strand10-1892
β-strand2117
β-strand2317
β-strand27-41152
β-strand4516
α-helix53-542
β-strand55-5958
β-strand62-6549
β-strand68110
α-helix691
α-helix72-732
β-strand79110
β-strand82-8549
β-strand88-9258
β-strand98-10142

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Human chorionic gonadotropinAprotein92Homo sapiensP01215 (AlphaFold model)
Human chorionic gonadotropinBprotein145P0DN86 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1HRP_1 HUMAN CHORIONIC GONADOTROPIN (chains A)
APDTQDCPECTLQENPFFSQPGAPILQCMGCCFSRAYPTPLRSKKTMLVQKNVTSESTCC
VAKSYNRVTVMGGFKVENHTACHCSTCYYHKS
Sequence of entity 2 (B), FASTA
>1HRP_2 HUMAN CHORIONIC GONADOTROPIN (chains B)
SKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYR
DVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSS
SKAPPPSLPSPSRLPGPSDTPILPQ

Ligands and cofactors

IDNameFormulaCopies
NAG2-acetamido-2-deoxy-beta-D-glucopyranoseC8 H15 N O62

Primary citation

Crystal structure of human chorionic gonadotropin. Lapthorn, A.J., Harris, D.C., Littlejohn, A. et al. Nature (1994) 369:455-461. DOI 10.1038/369455a0 · PubMed

Other PDB entries of the same protein (UniProt P01215 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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