Research workbench
Crystal structure of the N-terminal lg-domain of shbg in complex with norgestrel
Analyse Crystal structure of the N-terminal lg-domain of shbg in complex with norgestrel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LHV
- Type
- protein
- Length
- 173 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sex hormone-binding globulin
- UniProt
- P04278
- Ligands
- NOG, CA, ZN
- Pockets
- 2 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sex hormone-binding globulin | protein | 173 | 5% helix, 49% strand | P04278 |
Ligands and binding sites
- NOG · 13-beta-ethyl-17-alpha-ethynyl-17-beta-hydroxygon-4-en-3-one · ligand · chains A
- CA · Calcium ion · metal · chains A
- ZN · Zinc ion · metal · chains A
- IPA · Isopropyl alcohol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 270 | 0.82 | 0.93 | 33 | NOG |
| 2 | 51 | 0.26 | 0.73 | 14 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1LHV · Crystal structure of the N-terminal lg-domain of shbg in complex with norgestrel · the same entry in another collection · chain A against A, TM-score 1.00
- P04278 · AlphaFold monomer V2.0 prediction for sex hormone-binding globulin (P04278) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P04278
- Elsewhere: RCSB PDB 1LHV · PDBe 1LHV · UniProt P04278
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