Research workbench
Structure of human chorionic gonadotropin at 2.6 ångströms resolution from mad analysis of the selenomethionyl protein
Analyse Structure of human chorionic gonadotropin at 2.6 ångströms resolution from mad… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HCN
- Type
- protein
- Length
- 195 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P01215, P01233
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 85 | — | P01215 |
| B | — | protein | 110 | — | P01233 |
Compared structures
- 1HCN · Structure of human chorionic gonadotropin at 2.6 ångströms resolution from mad analysis… · the same entry in another collection · chain A against A, TM-score 1.00
- P01215 · AlphaFold monomer V2.0 prediction for glycoprotein hormones alpha chain (P01215) · a predicted model of the same protein · chain A against A, TM-score 0.94
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P01215
- Every structure of UniProt P01233
- Elsewhere: RCSB PDB 1HCN · PDBe 1HCN · UniProt P01215 · UniProt P01233
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